---
_id: '8971'
abstract:
- lang: eng
text: The actin-related protein (Arp)2/3 complex nucleates branched actin filament
networks pivotal for cell migration, endocytosis and pathogen infection. Its activation
is tightly regulated and involves complex structural rearrangements and actin
filament binding, which are yet to be understood. Here, we report a 9.0 Å resolution
structure of the actin filament Arp2/3 complex branch junction in cells using
cryo-electron tomography and subtomogram averaging. This allows us to generate
an accurate model of the active Arp2/3 complex in the branch junction and its
interaction with actin filaments. Notably, our model reveals a previously undescribed
set of interactions of the Arp2/3 complex with the mother filament, significantly
different to the previous branch junction model. Our structure also indicates
a central role for the ArpC3 subunit in stabilizing the active conformation.
acknowledged_ssus:
- _id: ScienComp
- _id: LifeSc
- _id: Bio
- _id: EM-Fac
acknowledgement: "This research was supported by the Scientific Service Units (SSUs)
of IST Austria through resources provided by Scientific Computing (SciComp), the
Life Science Facility (LSF), the BioImaging Facility (BIF), and the Electron Microscopy
Facility (EMF). We also thank Dimitry Tegunov (MPI for Biophysical Chemistry) for
helpful discussions\r\nabout the M software, and Michael Sixt (IST Austria) and
Klemens Rottner (Technical University Braunschweig, HZI Braunschweig) for critical
reading of the manuscript. We also thank Gregory Voth (University of Chicago) for
providing us the MD-derived branch junction model for comparison. The authors acknowledge
support from IST Austria and from the Austrian Science Fund (FWF): M02495 to G.D.
and Austrian Science Fund (FWF): P33367 to F.K.M.S. "
article_number: '6437'
article_processing_charge: No
article_type: original
author:
- first_name: Florian
full_name: Fäßler, Florian
id: 404F5528-F248-11E8-B48F-1D18A9856A87
last_name: Fäßler
orcid: 0000-0001-7149-769X
- first_name: Georgi A
full_name: Dimchev, Georgi A
id: 38C393BE-F248-11E8-B48F-1D18A9856A87
last_name: Dimchev
orcid: 0000-0001-8370-6161
- first_name: Victor-Valentin
full_name: Hodirnau, Victor-Valentin
id: 3661B498-F248-11E8-B48F-1D18A9856A87
last_name: Hodirnau
- first_name: William
full_name: Wan, William
last_name: Wan
- first_name: Florian KM
full_name: Schur, Florian KM
id: 48AD8942-F248-11E8-B48F-1D18A9856A87
last_name: Schur
orcid: 0000-0003-4790-8078
citation:
ama: Fäßler F, Dimchev GA, Hodirnau V-V, Wan W, Schur FK. Cryo-electron tomography
structure of Arp2/3 complex in cells reveals new insights into the branch junction.
Nature Communications. 2020;11. doi:10.1038/s41467-020-20286-x
apa: Fäßler, F., Dimchev, G. A., Hodirnau, V.-V., Wan, W., & Schur, F. K. (2020).
Cryo-electron tomography structure of Arp2/3 complex in cells reveals new insights
into the branch junction. Nature Communications. Springer Nature. https://doi.org/10.1038/s41467-020-20286-x
chicago: Fäßler, Florian, Georgi A Dimchev, Victor-Valentin Hodirnau, William Wan,
and Florian KM Schur. “Cryo-Electron Tomography Structure of Arp2/3 Complex in
Cells Reveals New Insights into the Branch Junction.” Nature Communications.
Springer Nature, 2020. https://doi.org/10.1038/s41467-020-20286-x.
ieee: F. Fäßler, G. A. Dimchev, V.-V. Hodirnau, W. Wan, and F. K. Schur, “Cryo-electron
tomography structure of Arp2/3 complex in cells reveals new insights into the
branch junction,” Nature Communications, vol. 11. Springer Nature, 2020.
ista: Fäßler F, Dimchev GA, Hodirnau V-V, Wan W, Schur FK. 2020. Cryo-electron tomography
structure of Arp2/3 complex in cells reveals new insights into the branch junction.
Nature Communications. 11, 6437.
mla: Fäßler, Florian, et al. “Cryo-Electron Tomography Structure of Arp2/3 Complex
in Cells Reveals New Insights into the Branch Junction.” Nature Communications,
vol. 11, 6437, Springer Nature, 2020, doi:10.1038/s41467-020-20286-x.
short: F. Fäßler, G.A. Dimchev, V.-V. Hodirnau, W. Wan, F.K. Schur, Nature Communications
11 (2020).
date_created: 2020-12-23T08:25:45Z
date_published: 2020-12-22T00:00:00Z
date_updated: 2023-08-24T11:01:50Z
day: '22'
ddc:
- '570'
department:
- _id: FlSc
- _id: EM-Fac
doi: 10.1038/s41467-020-20286-x
external_id:
isi:
- '000603078000003'
file:
- access_level: open_access
checksum: 55d43ea0061cc4027ba45e966e1db8cc
content_type: application/pdf
creator: dernst
date_created: 2020-12-28T08:16:10Z
date_updated: 2020-12-28T08:16:10Z
file_id: '8975'
file_name: 2020_NatureComm_Faessler.pdf
file_size: 3958727
relation: main_file
success: 1
file_date_updated: 2020-12-28T08:16:10Z
has_accepted_license: '1'
intvolume: ' 11'
isi: 1
keyword:
- General Biochemistry
- Genetics and Molecular Biology
- General Physics and Astronomy
- General Chemistry
language:
- iso: eng
month: '12'
oa: 1
oa_version: Published Version
project:
- _id: 9B954C5C-BA93-11EA-9121-9846C619BF3A
grant_number: P33367
name: Structure and isoform diversity of the Arp2/3 complex
- _id: 2674F658-B435-11E9-9278-68D0E5697425
call_identifier: FWF
grant_number: M02495
name: Protein structure and function in filopodia across scales
publication: Nature Communications
publication_identifier:
issn:
- 2041-1723
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
related_material:
link:
- description: News on IST Homepage
relation: press_release
url: https://ist.ac.at/en/news/cutting-edge-technology-reveals-structures-within-cells/
scopus_import: '1'
status: public
title: Cryo-electron tomography structure of Arp2/3 complex in cells reveals new insights
into the branch junction
tmp:
image: /images/cc_by.png
legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
short: CC BY (4.0)
type: journal_article
user_id: 4359f0d1-fa6c-11eb-b949-802e58b17ae8
volume: 11
year: '2020'
...
---
_id: '13361'
abstract:
- lang: eng
text: "In nature, light is harvested by photoactive proteins to drive a range of
biological processes, including photosynthesis, phototaxis, vision, and ultimately
life. Bacteriorhodopsin, for example, is a protein embedded within archaeal cell
membranes that binds the chromophore retinal within its hydrophobic pocket. Exposure
to light triggers regioselective photoisomerization of the confined retinal, which
in turn initiates a cascade of conformational changes within the protein, triggering
proton flux against the concentration gradient, providing the microorganisms with
the energy to live. We are inspired by these functions in nature to harness light
energy using synthetic photoswitches under confinement. Like retinal, synthetic
photoswitches require some degree of conformational flexibility to isomerize.
In nature, the conformational change associated with retinal isomerization is
accommodated by the structural flexibility of the opsin host, yet it results in
steric communication between the chromophore and the protein. Similarly, we strive
to design systems wherein isomerization of confined photoswitches results in steric
communication between a photoswitch and its confining environment. To achieve
this aim, a balance must be struck between molecular crowding and conformational
freedom under confinement: too much crowding prevents switching, whereas too much
freedom resembles switching of isolated molecules in solution, preventing communication.\r\n\r\nIn
this Account, we discuss five classes of synthetic light-switchable compounds—diarylethenes,
anthracenes, azobenzenes, spiropyrans, and donor–acceptor Stenhouse adducts—comparing
their behaviors under confinement and in solution. The environments employed to
confine these photoswitches are diverse, ranging from planar surfaces to nanosized
cavities within coordination cages, nanoporous frameworks, and nanoparticle aggregates.
The trends that emerge are primarily dependent on the nature of the photoswitch
and not on the material used for confinement. In general, we find that photoswitches
requiring less conformational freedom for switching are, as expected, more straightforward
to isomerize reversibly under confinement. Because these compounds undergo only
small structural changes upon isomerization, however, switching does not propagate
into communication with their environment. Conversely, photoswitches that require
more conformational freedom are more challenging to switch under confinement but
also can influence system-wide behavior.\r\n\r\nAlthough we are primarily interested
in the effects of geometric constraints on photoswitching under confinement, additional
effects inevitably emerge when a compound is removed from solution and placed
within a new, more crowded environment. For instance, we have found that compounds
that convert to zwitterionic isomers upon light irradiation often experience stabilization
of these forms under confinement. This effect results from the mutual stabilization
of zwitterions that are brought into close proximity on surfaces or within cavities.
Furthermore, photoswitches can experience preorganization under confinement, influencing
the selectivity and efficiency of their photoreactions. Because intermolecular
interactions arising from confinement cannot be considered independently from
the effects of geometric constraints, we describe all confinement effects concurrently
throughout this Account."
article_processing_charge: No
article_type: original
author:
- first_name: Angela B.
full_name: Grommet, Angela B.
last_name: Grommet
- first_name: Lucia M.
full_name: Lee, Lucia M.
last_name: Lee
- first_name: Rafal
full_name: Klajn, Rafal
id: 8e84690e-1e48-11ed-a02b-a1e6fb8bb53b
last_name: Klajn
citation:
ama: Grommet AB, Lee LM, Klajn R. Molecular photoswitching in confined spaces. Accounts
of Chemical Research. 2020;53(11):2600-2610. doi:10.1021/acs.accounts.0c00434
apa: Grommet, A. B., Lee, L. M., & Klajn, R. (2020). Molecular photoswitching
in confined spaces. Accounts of Chemical Research. American Chemical Society.
https://doi.org/10.1021/acs.accounts.0c00434
chicago: Grommet, Angela B., Lucia M. Lee, and Rafal Klajn. “Molecular Photoswitching
in Confined Spaces.” Accounts of Chemical Research. American Chemical Society,
2020. https://doi.org/10.1021/acs.accounts.0c00434.
ieee: A. B. Grommet, L. M. Lee, and R. Klajn, “Molecular photoswitching in confined
spaces,” Accounts of Chemical Research, vol. 53, no. 11. American Chemical
Society, pp. 2600–2610, 2020.
ista: Grommet AB, Lee LM, Klajn R. 2020. Molecular photoswitching in confined spaces.
Accounts of Chemical Research. 53(11), 2600–2610.
mla: Grommet, Angela B., et al. “Molecular Photoswitching in Confined Spaces.” Accounts
of Chemical Research, vol. 53, no. 11, American Chemical Society, 2020, pp.
2600–10, doi:10.1021/acs.accounts.0c00434.
short: A.B. Grommet, L.M. Lee, R. Klajn, Accounts of Chemical Research 53 (2020)
2600–2610.
date_created: 2023-08-01T09:35:50Z
date_published: 2020-11-17T00:00:00Z
date_updated: 2023-08-07T10:06:46Z
day: '17'
doi: 10.1021/acs.accounts.0c00434
extern: '1'
external_id:
pmid:
- '32969638'
intvolume: ' 53'
issue: '11'
keyword:
- General Medicine
- General Chemistry
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1021/acs.accounts.0c00434
month: '11'
oa: 1
oa_version: Published Version
page: 2600-2610
pmid: 1
publication: Accounts of Chemical Research
publication_identifier:
eissn:
- 1520-4898
issn:
- 0001-4842
publication_status: published
publisher: American Chemical Society
quality_controlled: '1'
scopus_import: '1'
status: public
title: Molecular photoswitching in confined spaces
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 53
year: '2020'
...
---
_id: '13362'
abstract:
- lang: eng
text: Aggregation of organic molecules can drastically affect their physicochemical
properties. For instance, the optical properties of BODIPY dyes are inherently
related to the degree of aggregation and the mutual orientation of BODIPY units
within these aggregates. Whereas the noncovalent aggregation of various BODIPY
dyes has been studied in diverse media, the ill-defined nature of these aggregates
has made it difficult to elucidate the structure–property relationships. Here,
we studied the encapsulation of three structurally simple BODIPY derivatives within
the hydrophobic cavity of a water-soluble, flexible PdII6L4 coordination cage.
The cavity size allowed for the selective encapsulation of two dye molecules,
irrespective of the substitution pattern on the BODIPY core. Working with a model,
a pentamethyl-substituted derivative, we found that the mutual orientation of
two BODIPY units in the cage’s cavity was remarkably similar to that in the crystalline
state of the free dye, allowing us to isolate and characterize the smallest possible
noncovalent H-type BODIPY aggregate, namely, an H-dimer. Interestingly, a CF3-substituted
BODIPY, known for forming J-type aggregates, was also encapsulated as an H-dimer.
Taking advantage of the dynamic nature of encapsulation, we developed a system
in which reversible switching between H- and J-aggregates can be induced for multiple
cycles simply by addition and subsequent destruction of the cage. We expect that
the ability to rapidly and reversibly manipulate the optical properties of supramolecular
inclusion complexes in aqueous media will open up avenues for developing detection
systems that operate within biological environments.
article_processing_charge: No
article_type: original
author:
- first_name: Julius
full_name: Gemen, Julius
last_name: Gemen
- first_name: Johannes
full_name: Ahrens, Johannes
last_name: Ahrens
- first_name: Linda J. W.
full_name: Shimon, Linda J. W.
last_name: Shimon
- first_name: Rafal
full_name: Klajn, Rafal
id: 8e84690e-1e48-11ed-a02b-a1e6fb8bb53b
last_name: Klajn
citation:
ama: Gemen J, Ahrens J, Shimon LJW, Klajn R. Modulating the optical properties of
BODIPY dyes by noncovalent dimerization within a flexible coordination cage. Journal
of the American Chemical Society. 2020;142(41):17721-17729. doi:10.1021/jacs.0c08589
apa: Gemen, J., Ahrens, J., Shimon, L. J. W., & Klajn, R. (2020). Modulating
the optical properties of BODIPY dyes by noncovalent dimerization within a flexible
coordination cage. Journal of the American Chemical Society. American Chemical
Society. https://doi.org/10.1021/jacs.0c08589
chicago: Gemen, Julius, Johannes Ahrens, Linda J. W. Shimon, and Rafal Klajn. “Modulating
the Optical Properties of BODIPY Dyes by Noncovalent Dimerization within a Flexible
Coordination Cage.” Journal of the American Chemical Society. American
Chemical Society, 2020. https://doi.org/10.1021/jacs.0c08589.
ieee: J. Gemen, J. Ahrens, L. J. W. Shimon, and R. Klajn, “Modulating the optical
properties of BODIPY dyes by noncovalent dimerization within a flexible coordination
cage,” Journal of the American Chemical Society, vol. 142, no. 41. American
Chemical Society, pp. 17721–17729, 2020.
ista: Gemen J, Ahrens J, Shimon LJW, Klajn R. 2020. Modulating the optical properties
of BODIPY dyes by noncovalent dimerization within a flexible coordination cage.
Journal of the American Chemical Society. 142(41), 17721–17729.
mla: Gemen, Julius, et al. “Modulating the Optical Properties of BODIPY Dyes by
Noncovalent Dimerization within a Flexible Coordination Cage.” Journal of the
American Chemical Society, vol. 142, no. 41, American Chemical Society, 2020,
pp. 17721–29, doi:10.1021/jacs.0c08589.
short: J. Gemen, J. Ahrens, L.J.W. Shimon, R. Klajn, Journal of the American Chemical
Society 142 (2020) 17721–17729.
date_created: 2023-08-01T09:36:10Z
date_published: 2020-10-04T00:00:00Z
date_updated: 2023-08-07T10:09:54Z
day: '04'
doi: 10.1021/jacs.0c08589
extern: '1'
external_id:
pmid:
- '33006898'
intvolume: ' 142'
issue: '41'
keyword:
- Colloid and Surface Chemistry
- Biochemistry
- General Chemistry
- Catalysis
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1021/jacs.0c08589
month: '10'
oa: 1
oa_version: Published Version
page: 17721-17729
pmid: 1
publication: Journal of the American Chemical Society
publication_identifier:
eissn:
- 1520-5126
issn:
- 0002-7863
publication_status: published
publisher: American Chemical Society
quality_controlled: '1'
scopus_import: '1'
status: public
title: Modulating the optical properties of BODIPY dyes by noncovalent dimerization
within a flexible coordination cage
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 142
year: '2020'
...
---
_id: '13363'
abstract:
- lang: eng
text: Temporal activation of biological processes by visible light and subsequent
return to an inactive state in the absence of light is an essential characteristic
of photoreceptor cells. Inspired by these phenomena, light-responsive materials
are very attractive due to the high spatiotemporal control of light irradiation,
with light being able to precisely orchestrate processes repeatedly over many
cycles. Herein, it is reported that light-driven proton transfer triggered by
a merocyanine-based photoacid can be used to modulate the permeability of pH-responsive
polymersomes through cyclic, temporally controlled protonation and deprotonation
of the polymersome membrane. The membranes can undergo repeated light-driven swelling–contraction
cycles without losing functional effectiveness. When applied to enzyme loaded-nanoreactors,
this membrane responsiveness is used for the reversible control of enzymatic reactions.
This combination of the merocyanine-based photoacid and pH-switchable nanoreactors
results in rapidly responding and versatile supramolecular systems successfully
used to switch enzymatic reactions ON and OFF on demand.
article_number: '2002135'
article_processing_charge: No
article_type: original
author:
- first_name: Silvia
full_name: Moreno, Silvia
last_name: Moreno
- first_name: Priyanka
full_name: Sharan, Priyanka
last_name: Sharan
- first_name: Johanna
full_name: Engelke, Johanna
last_name: Engelke
- first_name: Hannes
full_name: Gumz, Hannes
last_name: Gumz
- first_name: Susanne
full_name: Boye, Susanne
last_name: Boye
- first_name: Ulrich
full_name: Oertel, Ulrich
last_name: Oertel
- first_name: Peng
full_name: Wang, Peng
last_name: Wang
- first_name: Susanta
full_name: Banerjee, Susanta
last_name: Banerjee
- first_name: Rafal
full_name: Klajn, Rafal
id: 8e84690e-1e48-11ed-a02b-a1e6fb8bb53b
last_name: Klajn
- first_name: Brigitte
full_name: Voit, Brigitte
last_name: Voit
- first_name: Albena
full_name: Lederer, Albena
last_name: Lederer
- first_name: Dietmar
full_name: Appelhans, Dietmar
last_name: Appelhans
citation:
ama: Moreno S, Sharan P, Engelke J, et al. Light‐driven proton transfer for cyclic
and temporal switching of enzymatic nanoreactors. Small. 2020;16(37). doi:10.1002/smll.202002135
apa: Moreno, S., Sharan, P., Engelke, J., Gumz, H., Boye, S., Oertel, U., … Appelhans,
D. (2020). Light‐driven proton transfer for cyclic and temporal switching of enzymatic
nanoreactors. Small. Wiley. https://doi.org/10.1002/smll.202002135
chicago: Moreno, Silvia, Priyanka Sharan, Johanna Engelke, Hannes Gumz, Susanne
Boye, Ulrich Oertel, Peng Wang, et al. “Light‐driven Proton Transfer for Cyclic
and Temporal Switching of Enzymatic Nanoreactors.” Small. Wiley, 2020.
https://doi.org/10.1002/smll.202002135.
ieee: S. Moreno et al., “Light‐driven proton transfer for cyclic and temporal
switching of enzymatic nanoreactors,” Small, vol. 16, no. 37. Wiley, 2020.
ista: Moreno S, Sharan P, Engelke J, Gumz H, Boye S, Oertel U, Wang P, Banerjee
S, Klajn R, Voit B, Lederer A, Appelhans D. 2020. Light‐driven proton transfer
for cyclic and temporal switching of enzymatic nanoreactors. Small. 16(37), 2002135.
mla: Moreno, Silvia, et al. “Light‐driven Proton Transfer for Cyclic and Temporal
Switching of Enzymatic Nanoreactors.” Small, vol. 16, no. 37, 2002135,
Wiley, 2020, doi:10.1002/smll.202002135.
short: S. Moreno, P. Sharan, J. Engelke, H. Gumz, S. Boye, U. Oertel, P. Wang, S.
Banerjee, R. Klajn, B. Voit, A. Lederer, D. Appelhans, Small 16 (2020).
date_created: 2023-08-01T09:36:48Z
date_published: 2020-08-11T00:00:00Z
date_updated: 2023-08-07T10:11:41Z
day: '11'
doi: 10.1002/smll.202002135
extern: '1'
external_id:
pmid:
- '32783385'
intvolume: ' 16'
issue: '37'
keyword:
- Biomaterials
- Biotechnology
- General Materials Science
- General Chemistry
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1002/smll.202002135
month: '08'
oa: 1
oa_version: Published Version
pmid: 1
publication: Small
publication_identifier:
eissn:
- 1613-6829
issn:
- 1613-6810
publication_status: published
publisher: Wiley
quality_controlled: '1'
scopus_import: '1'
status: public
title: Light‐driven proton transfer for cyclic and temporal switching of enzymatic
nanoreactors
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 16
year: '2020'
...
---
_id: '13364'
abstract:
- lang: eng
text: Photochromic molecules undergo reversible isomerization upon irradiation with
light at different wavelengths, a process that can alter their physical and chemical
properties. For instance, dihydropyrene (DHP) is a deep-colored compound that
isomerizes to light-brown cyclophanediene (CPD) upon irradiation with visible
light. CPD can then isomerize back to DHP upon irradiation with UV light or thermally
in the dark. Conversion between DHP and CPD is thought to proceed via a biradical
intermediate; bimolecular events involving this unstable intermediate thus result
in rapid decomposition and poor cycling performance. Here, we show that the reversible
isomerization of DHP can be stabilized upon confinement within a PdII6L4 coordination
cage. By protecting this reactive intermediate using the cage, each isomerization
reaction proceeds to higher yield, which significantly decreases the fatigue experienced
by the system upon repeated photocycling. Although molecular confinement is known
to help stabilize reactive species, this effect is not typically employed to protect
reactive intermediates and thus improve reaction yields. We envisage that performing
reactions under confinement will not only improve the cyclic performance of photochromic
molecules, but may also increase the amount of product obtainable from traditionally
low-yielding organic reactions.
article_processing_charge: No
article_type: original
author:
- first_name: Martina
full_name: Canton, Martina
last_name: Canton
- first_name: Angela B.
full_name: Grommet, Angela B.
last_name: Grommet
- first_name: Luca
full_name: Pesce, Luca
last_name: Pesce
- first_name: Julius
full_name: Gemen, Julius
last_name: Gemen
- first_name: Shiming
full_name: Li, Shiming
last_name: Li
- first_name: Yael
full_name: Diskin-Posner, Yael
last_name: Diskin-Posner
- first_name: Alberto
full_name: Credi, Alberto
last_name: Credi
- first_name: Giovanni M.
full_name: Pavan, Giovanni M.
last_name: Pavan
- first_name: Joakim
full_name: Andréasson, Joakim
last_name: Andréasson
- first_name: Rafal
full_name: Klajn, Rafal
id: 8e84690e-1e48-11ed-a02b-a1e6fb8bb53b
last_name: Klajn
citation:
ama: Canton M, Grommet AB, Pesce L, et al. Improving fatigue resistance of dihydropyrene
by encapsulation within a coordination cage. Journal of the American Chemical
Society. 2020;142(34):14557-14565. doi:10.1021/jacs.0c06146
apa: Canton, M., Grommet, A. B., Pesce, L., Gemen, J., Li, S., Diskin-Posner, Y.,
… Klajn, R. (2020). Improving fatigue resistance of dihydropyrene by encapsulation
within a coordination cage. Journal of the American Chemical Society. American
Chemical Society. https://doi.org/10.1021/jacs.0c06146
chicago: Canton, Martina, Angela B. Grommet, Luca Pesce, Julius Gemen, Shiming Li,
Yael Diskin-Posner, Alberto Credi, Giovanni M. Pavan, Joakim Andréasson, and Rafal
Klajn. “Improving Fatigue Resistance of Dihydropyrene by Encapsulation within
a Coordination Cage.” Journal of the American Chemical Society. American
Chemical Society, 2020. https://doi.org/10.1021/jacs.0c06146.
ieee: M. Canton et al., “Improving fatigue resistance of dihydropyrene by
encapsulation within a coordination cage,” Journal of the American Chemical
Society, vol. 142, no. 34. American Chemical Society, pp. 14557–14565, 2020.
ista: Canton M, Grommet AB, Pesce L, Gemen J, Li S, Diskin-Posner Y, Credi A, Pavan
GM, Andréasson J, Klajn R. 2020. Improving fatigue resistance of dihydropyrene
by encapsulation within a coordination cage. Journal of the American Chemical
Society. 142(34), 14557–14565.
mla: Canton, Martina, et al. “Improving Fatigue Resistance of Dihydropyrene by Encapsulation
within a Coordination Cage.” Journal of the American Chemical Society,
vol. 142, no. 34, American Chemical Society, 2020, pp. 14557–65, doi:10.1021/jacs.0c06146.
short: M. Canton, A.B. Grommet, L. Pesce, J. Gemen, S. Li, Y. Diskin-Posner, A.
Credi, G.M. Pavan, J. Andréasson, R. Klajn, Journal of the American Chemical Society
142 (2020) 14557–14565.
date_created: 2023-08-01T09:36:59Z
date_published: 2020-08-14T00:00:00Z
date_updated: 2023-08-07T10:15:38Z
day: '14'
doi: 10.1021/jacs.0c06146
extern: '1'
external_id:
pmid:
- '32791832'
intvolume: ' 142'
issue: '34'
keyword:
- Colloid and Surface Chemistry
- Biochemistry
- General Chemistry
- Catalysis
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1021/jacs.0c06146
month: '08'
oa: 1
oa_version: Published Version
page: 14557-14565
pmid: 1
publication: Journal of the American Chemical Society
publication_identifier:
eissn:
- 1520-5126
issn:
- 0002-7863
publication_status: published
publisher: American Chemical Society
quality_controlled: '1'
scopus_import: '1'
status: public
title: Improving fatigue resistance of dihydropyrene by encapsulation within a coordination
cage
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 142
year: '2020'
...
---
_id: '13365'
abstract:
- lang: eng
text: Photoswitchable molecules are employed for many applications, from the development
of active materials to the design of stimuli-responsive molecular systems and
light-powered molecular machines. To fully exploit their potential, we must learn
ways to control the mechanism and kinetics of their photoinduced isomerization.
One possible strategy involves confinement of photoresponsive switches such as
azobenzenes or spiropyrans within crowded molecular environments, which may allow
control over their light-induced conversion. However, the molecular factors that
influence and control the switching process under realistic conditions and within
dynamic molecular regimes often remain difficult to ascertain. As a case study,
here we have employed molecular models to probe the isomerization of azobenzene
guests within a Pd(II)-based coordination cage host in water. Atomistic molecular
dynamics and metadynamics simulations allow us to characterize the flexibility
of the cage in the solvent, the (rare) guest encapsulation and release events,
and the relative probability/kinetics of light-induced isomerization of azobenzene
analogues in these host–guest systems. In this way, we can reconstruct the mechanism
of azobenzene switching inside the cage cavity and explore key molecular factors
that may control this event. We obtain a molecular-level insight on the effects
of crowding and host–guest interactions on azobenzene isomerization. The detailed
picture elucidated by this study may enable the rational design of photoswitchable
systems whose reactivity can be controlled via host–guest interactions.
article_processing_charge: No
article_type: original
author:
- first_name: Luca
full_name: Pesce, Luca
last_name: Pesce
- first_name: Claudio
full_name: Perego, Claudio
last_name: Perego
- first_name: Angela B.
full_name: Grommet, Angela B.
last_name: Grommet
- first_name: Rafal
full_name: Klajn, Rafal
id: 8e84690e-1e48-11ed-a02b-a1e6fb8bb53b
last_name: Klajn
- first_name: Giovanni M.
full_name: Pavan, Giovanni M.
last_name: Pavan
citation:
ama: Pesce L, Perego C, Grommet AB, Klajn R, Pavan GM. Molecular factors controlling
the isomerization of Azobenzenes in the cavity of a flexible coordination cage.
Journal of the American Chemical Society. 2020;142(21):9792-9802. doi:10.1021/jacs.0c03444
apa: Pesce, L., Perego, C., Grommet, A. B., Klajn, R., & Pavan, G. M. (2020).
Molecular factors controlling the isomerization of Azobenzenes in the cavity of
a flexible coordination cage. Journal of the American Chemical Society.
American Chemical Society. https://doi.org/10.1021/jacs.0c03444
chicago: Pesce, Luca, Claudio Perego, Angela B. Grommet, Rafal Klajn, and Giovanni
M. Pavan. “Molecular Factors Controlling the Isomerization of Azobenzenes in the
Cavity of a Flexible Coordination Cage.” Journal of the American Chemical Society.
American Chemical Society, 2020. https://doi.org/10.1021/jacs.0c03444.
ieee: L. Pesce, C. Perego, A. B. Grommet, R. Klajn, and G. M. Pavan, “Molecular
factors controlling the isomerization of Azobenzenes in the cavity of a flexible
coordination cage,” Journal of the American Chemical Society, vol. 142,
no. 21. American Chemical Society, pp. 9792–9802, 2020.
ista: Pesce L, Perego C, Grommet AB, Klajn R, Pavan GM. 2020. Molecular factors
controlling the isomerization of Azobenzenes in the cavity of a flexible coordination
cage. Journal of the American Chemical Society. 142(21), 9792–9802.
mla: Pesce, Luca, et al. “Molecular Factors Controlling the Isomerization of Azobenzenes
in the Cavity of a Flexible Coordination Cage.” Journal of the American Chemical
Society, vol. 142, no. 21, American Chemical Society, 2020, pp. 9792–802,
doi:10.1021/jacs.0c03444.
short: L. Pesce, C. Perego, A.B. Grommet, R. Klajn, G.M. Pavan, Journal of the American
Chemical Society 142 (2020) 9792–9802.
date_created: 2023-08-01T09:37:12Z
date_published: 2020-04-30T00:00:00Z
date_updated: 2023-08-07T10:18:53Z
day: '30'
doi: 10.1021/jacs.0c03444
extern: '1'
external_id:
pmid:
- '32353237'
intvolume: ' 142'
issue: '21'
keyword:
- Colloid and Surface Chemistry
- Biochemistry
- General Chemistry
- Catalysis
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1021/jacs.0c03444
month: '04'
oa: 1
oa_version: Published Version
page: 9792-9802
pmid: 1
publication: Journal of the American Chemical Society
publication_identifier:
eissn:
- 1520-5126
issn:
- 0002-7863
publication_status: published
publisher: American Chemical Society
quality_controlled: '1'
scopus_import: '1'
status: public
title: Molecular factors controlling the isomerization of Azobenzenes in the cavity
of a flexible coordination cage
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 142
year: '2020'
...
---
_id: '9054'
abstract:
- lang: eng
text: 'The fundamental and practical importance of particle stabilization has motivated
various characterization methods for studying polymer brushes on particle surfaces.
In this work, we show how one can perform sensitive measurements of neutral polymer
coating on colloidal particles using a commercial zetameter and salt solutions.
By systematically varying the Debye length, we study the mobility of the polymer-coated
particles in an applied electric field and show that the electrophoretic mobility
of polymer-coated particles normalized by the mobility of non-coated particles
is entirely controlled by the polymer brush and independent of the native surface
charge, here controlled with pH, or the surface–ion interaction. Our result is
rationalized with a simple hydrodynamic model, allowing for the estimation of
characteristics of the polymer coating: the brush length L, and the Brinkman length
ξ, determined by its resistance to flows. We demonstrate that the Debye layer
provides a convenient and faithful probe to the characterization of polymer coatings
on particles. Because the method simply relies on a conventional zetameter, it
is widely accessible and offers a practical tool to rapidly probe neutral polymer
brushes, an asset in the development and utilization of polymer-coated colloidal
particles.'
article_processing_charge: No
article_type: original
author:
- first_name: Mena
full_name: Youssef, Mena
last_name: Youssef
- first_name: Alexandre
full_name: Morin, Alexandre
last_name: Morin
- first_name: Antoine
full_name: Aubret, Antoine
last_name: Aubret
- first_name: Stefano
full_name: Sacanna, Stefano
last_name: Sacanna
- first_name: Jérémie A
full_name: Palacci, Jérémie A
id: 8fb92548-2b22-11eb-b7c1-a3f0d08d7c7d
last_name: Palacci
orcid: 0000-0002-7253-9465
citation:
ama: Youssef M, Morin A, Aubret A, Sacanna S, Palacci JA. Rapid characterization
of neutral polymer brush with a conventional zetameter and a variable pinch of
salt. Soft Matter. 2020;16(17):4274-4282. doi:10.1039/c9sm01850f
apa: Youssef, M., Morin, A., Aubret, A., Sacanna, S., & Palacci, J. A. (2020).
Rapid characterization of neutral polymer brush with a conventional zetameter
and a variable pinch of salt. Soft Matter. Royal Society of Chemistry .
https://doi.org/10.1039/c9sm01850f
chicago: Youssef, Mena, Alexandre Morin, Antoine Aubret, Stefano Sacanna, and Jérémie
A Palacci. “Rapid Characterization of Neutral Polymer Brush with a Conventional
Zetameter and a Variable Pinch of Salt.” Soft Matter. Royal Society of
Chemistry , 2020. https://doi.org/10.1039/c9sm01850f.
ieee: M. Youssef, A. Morin, A. Aubret, S. Sacanna, and J. A. Palacci, “Rapid characterization
of neutral polymer brush with a conventional zetameter and a variable pinch of
salt,” Soft Matter, vol. 16, no. 17. Royal Society of Chemistry , pp. 4274–4282,
2020.
ista: Youssef M, Morin A, Aubret A, Sacanna S, Palacci JA. 2020. Rapid characterization
of neutral polymer brush with a conventional zetameter and a variable pinch of
salt. Soft Matter. 16(17), 4274–4282.
mla: Youssef, Mena, et al. “Rapid Characterization of Neutral Polymer Brush with
a Conventional Zetameter and a Variable Pinch of Salt.” Soft Matter, vol.
16, no. 17, Royal Society of Chemistry , 2020, pp. 4274–82, doi:10.1039/c9sm01850f.
short: M. Youssef, A. Morin, A. Aubret, S. Sacanna, J.A. Palacci, Soft Matter 16
(2020) 4274–4282.
date_created: 2021-02-01T13:45:11Z
date_published: 2020-05-07T00:00:00Z
date_updated: 2023-02-23T13:47:45Z
day: '07'
doi: 10.1039/c9sm01850f
extern: '1'
external_id:
pmid:
- '32307507'
intvolume: ' 16'
issue: '17'
keyword:
- General Chemistry
- Condensed Matter Physics
language:
- iso: eng
month: '05'
oa_version: None
page: 4274-4282
pmid: 1
publication: Soft Matter
publication_identifier:
eissn:
- 1744-6848
issn:
- 1744-683X
publication_status: published
publisher: 'Royal Society of Chemistry '
quality_controlled: '1'
scopus_import: '1'
status: public
title: Rapid characterization of neutral polymer brush with a conventional zetameter
and a variable pinch of salt
type: journal_article
user_id: D865714E-FA4E-11E9-B85B-F5C5E5697425
volume: 16
year: '2020'
...
---
_id: '9067'
abstract:
- lang: eng
text: Gadolinium silicide (Gd5Si4) nanoparticles are an interesting class of materials
due to their high magnetization, low Curie temperature, low toxicity in biological
environments and their multifunctional properties. We report the magnetic and
magnetothermal properties of gadolinium silicide (Gd5Si4) nanoparticles prepared
by surfactant-assisted ball milling of arc melted bulk ingots of the compound.
Using different milling times and speeds, a wide range of crystallite sizes (13–43
nm) could be produced and a reduction in Curie temperature (TC) from 340 K to
317 K was achieved, making these nanoparticles suitable for self-controlled magnetic
hyperthermia applications. The magnetothermal effect was measured in applied AC
magnetic fields of amplitude 164–239 Oe and frequencies 163–519 kHz. All particles
showed magnetic heating with a strong dependence of the specific absorption rate
(SAR) on the average crystallite size. The highest SAR of 3.7 W g−1 was measured
for 43 nm sized nanoparticles of Gd5Si4. The high SAR and low TC, (within the
therapeutic range for magnetothermal therapy) makes the Gd5Si4 behave like self-regulating
heat switches that would be suitable for self-controlled magnetic hyperthermia
applications after biocompatibility and cytotoxicity tests.
article_processing_charge: No
article_type: original
author:
- first_name: Muhammad
full_name: Nauman, Muhammad
id: 32c21954-2022-11eb-9d5f-af9f93c24e71
last_name: Nauman
orcid: 0000-0002-2111-4846
- first_name: Muhammad Hisham
full_name: Alnasir, Muhammad Hisham
last_name: Alnasir
- first_name: Muhammad Asif
full_name: Hamayun, Muhammad Asif
last_name: Hamayun
- first_name: YiXu
full_name: Wang, YiXu
last_name: Wang
- first_name: Michael
full_name: Shatruk, Michael
last_name: Shatruk
- first_name: Sadia
full_name: Manzoor, Sadia
last_name: Manzoor
citation:
ama: Nauman M, Alnasir MH, Hamayun MA, Wang Y, Shatruk M, Manzoor S. Size-dependent
magnetic and magnetothermal properties of gadolinium silicide nanoparticles. RSC
Advances. 2020;10(47):28383-28389. doi:10.1039/d0ra05394e
apa: Nauman, M., Alnasir, M. H., Hamayun, M. A., Wang, Y., Shatruk, M., & Manzoor,
S. (2020). Size-dependent magnetic and magnetothermal properties of gadolinium
silicide nanoparticles. RSC Advances. Royal Society of Chemistry. https://doi.org/10.1039/d0ra05394e
chicago: Nauman, Muhammad, Muhammad Hisham Alnasir, Muhammad Asif Hamayun, YiXu
Wang, Michael Shatruk, and Sadia Manzoor. “Size-Dependent Magnetic and Magnetothermal
Properties of Gadolinium Silicide Nanoparticles.” RSC Advances. Royal Society
of Chemistry, 2020. https://doi.org/10.1039/d0ra05394e.
ieee: M. Nauman, M. H. Alnasir, M. A. Hamayun, Y. Wang, M. Shatruk, and S. Manzoor,
“Size-dependent magnetic and magnetothermal properties of gadolinium silicide
nanoparticles,” RSC Advances, vol. 10, no. 47. Royal Society of Chemistry,
pp. 28383–28389, 2020.
ista: Nauman M, Alnasir MH, Hamayun MA, Wang Y, Shatruk M, Manzoor S. 2020. Size-dependent
magnetic and magnetothermal properties of gadolinium silicide nanoparticles. RSC
Advances. 10(47), 28383–28389.
mla: Nauman, Muhammad, et al. “Size-Dependent Magnetic and Magnetothermal Properties
of Gadolinium Silicide Nanoparticles.” RSC Advances, vol. 10, no. 47, Royal
Society of Chemistry, 2020, pp. 28383–89, doi:10.1039/d0ra05394e.
short: M. Nauman, M.H. Alnasir, M.A. Hamayun, Y. Wang, M. Shatruk, S. Manzoor, RSC
Advances 10 (2020) 28383–28389.
date_created: 2021-02-02T15:51:23Z
date_published: 2020-07-29T00:00:00Z
date_updated: 2021-02-04T07:16:37Z
day: '29'
doi: 10.1039/d0ra05394e
extern: '1'
intvolume: ' 10'
issue: '47'
keyword:
- General Chemistry
- General Chemical Engineering
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1039/d0ra05394e
month: '07'
oa: 1
oa_version: Published Version
page: 28383-28389
publication: RSC Advances
publication_identifier:
issn:
- 2046-2069
publication_status: published
publisher: Royal Society of Chemistry
quality_controlled: '1'
status: public
title: Size-dependent magnetic and magnetothermal properties of gadolinium silicide
nanoparticles
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 10
year: '2020'
...
---
_id: '10341'
abstract:
- lang: eng
text: Tracing the motion of macromolecules, viruses, and nanoparticles adsorbed
onto cell membranes is currently the most direct way of probing the complex dynamic
interactions behind vital biological processes, including cell signalling, trafficking,
and viral infection. The resulting trajectories are usually consistent with some
type of anomalous diffusion, but the molecular origins behind the observed anomalous
behaviour are usually not obvious. Here we use coarse-grained molecular dynamics
simulations to help identify the physical mechanisms that can give rise to experimentally
observed trajectories of nanoscopic objects moving on biological membranes. We
find that diffusion on membranes of high fluidities typically results in normal
diffusion of the adsorbed nanoparticle, irrespective of the concentration of receptors,
receptor clustering, or multivalent interactions between the particle and membrane
receptors. Gel-like membranes on the other hand result in anomalous diffusion
of the particle, which becomes more pronounced at higher receptor concentrations.
This anomalous diffusion is characterised by local particle trapping in the regions
of high receptor concentrations and fast hopping between such regions. The normal
diffusion is recovered in the limit where the gel membrane is saturated with receptors.
We conclude that hindered receptor diffusivity can be a common reason behind the
observed anomalous diffusion of viruses, vesicles, and nanoparticles adsorbed
on cell and model membranes. Our results enable direct comparison with experiments
and offer a new route for interpreting motility experiments on cell membranes.
acknowledgement: We thank Jessica McQuade for her input at the start of the project.
We acknowledge support from the ERASMUS Placement Programme (V. E. D.), the UCL
Institute for the Physics of Living Systems (V. E. D. and A. Š.), the UCL Global
Engagement Fund (L. M. C. J.), and the Royal Society (A. Š.).
article_processing_charge: No
article_type: original
author:
- first_name: V. E.
full_name: Debets, V. E.
last_name: Debets
- first_name: L. M. C.
full_name: Janssen, L. M. C.
last_name: Janssen
- first_name: Anđela
full_name: Šarić, Anđela
id: bf63d406-f056-11eb-b41d-f263a6566d8b
last_name: Šarić
orcid: 0000-0002-7854-2139
citation:
ama: Debets VE, Janssen LMC, Šarić A. Characterising the diffusion of biological
nanoparticles on fluid and cross-linked membranes. Soft Matter. 2020;16(47):10628-10639.
doi:10.1039/d0sm00712a
apa: Debets, V. E., Janssen, L. M. C., & Šarić, A. (2020). Characterising the
diffusion of biological nanoparticles on fluid and cross-linked membranes. Soft
Matter. Royal Society of Chemistry. https://doi.org/10.1039/d0sm00712a
chicago: Debets, V. E., L. M. C. Janssen, and Anđela Šarić. “Characterising the
Diffusion of Biological Nanoparticles on Fluid and Cross-Linked Membranes.” Soft
Matter. Royal Society of Chemistry, 2020. https://doi.org/10.1039/d0sm00712a.
ieee: V. E. Debets, L. M. C. Janssen, and A. Šarić, “Characterising the diffusion
of biological nanoparticles on fluid and cross-linked membranes,” Soft Matter,
vol. 16, no. 47. Royal Society of Chemistry, pp. 10628–10639, 2020.
ista: Debets VE, Janssen LMC, Šarić A. 2020. Characterising the diffusion of biological
nanoparticles on fluid and cross-linked membranes. Soft Matter. 16(47), 10628–10639.
mla: Debets, V. E., et al. “Characterising the Diffusion of Biological Nanoparticles
on Fluid and Cross-Linked Membranes.” Soft Matter, vol. 16, no. 47, Royal
Society of Chemistry, 2020, pp. 10628–39, doi:10.1039/d0sm00712a.
short: V.E. Debets, L.M.C. Janssen, A. Šarić, Soft Matter 16 (2020) 10628–10639.
date_created: 2021-11-26T06:29:41Z
date_published: 2020-10-06T00:00:00Z
date_updated: 2021-11-26T07:00:33Z
day: '06'
doi: 10.1039/d0sm00712a
extern: '1'
external_id:
pmid:
- '33084724'
intvolume: ' 16'
issue: '47'
keyword:
- condensed matter physics
- general chemistry
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://www.biorxiv.org/content/10.1101/2020.05.01.071761v1
month: '10'
oa: 1
oa_version: Published Version
page: 10628-10639
pmid: 1
publication: Soft Matter
publication_identifier:
issn:
- 1744-683X
- 1744-6848
publication_status: published
publisher: Royal Society of Chemistry
quality_controlled: '1'
scopus_import: '1'
status: public
title: Characterising the diffusion of biological nanoparticles on fluid and cross-linked
membranes
type: journal_article
user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9
volume: 16
year: '2020'
...
---
_id: '10350'
abstract:
- lang: eng
text: The misfolding and aberrant aggregation of proteins into fibrillar structures
is a key factor in some of the most prevalent human diseases, including diabetes
and dementia. Low molecular weight oligomers are thought to be a central factor
in the pathology of these diseases, as well as critical intermediates in the fibril
formation process, and as such have received much recent attention. Moreover,
on-pathway oligomeric intermediates are potential targets for therapeutic strategies
aimed at interrupting the fibril formation process. However, a consistent framework
for distinguishing on-pathway from off-pathway oligomers has hitherto been lacking
and, in particular, no consensus definition of on- and off-pathway oligomers is
available. In this paper, we argue that a non-binary definition of oligomers'
contribution to fibril-forming pathways may be more informative and we suggest
a quantitative framework, in which each oligomeric species is assigned a value
between 0 and 1 describing its relative contribution to the formation of fibrils.
First, we clarify the distinction between oligomers and fibrils, and then we use
the formalism of reaction networks to develop a general definition for on-pathway
oligomers, that yields meaningful classifications in the context of amyloid formation.
By applying these concepts to Monte Carlo simulations of a minimal aggregating
system, and by revisiting several previous studies of amyloid oligomers in light
of our new framework, we demonstrate how to perform these classifications in practice.
For each oligomeric species we obtain the degree to which it is on-pathway, highlighting
the most effective pharmaceutical targets for the inhibition of amyloid fibril
formation.
acknowledgement: We are grateful to the Schiff Foundation (AJD), Peterhouse, Cambridge
(TCTM), the Swiss National Science foundation (TCTM), Ramon Jenkins Fellowship,
Sidney Sussex, Cambridge (GM), the Royal Society (AŠ), the Academy of Medical Sciences
and Wellcome Trust (AŠ), the Danish Research Council (MK), the Lundbeck Foundation
(MK), the Swedish Research Council (SL), the Wellcome Trust (TPJK), the Cambridge
Centre for Misfolding Diseases (TPJK), the BBSRC (TPJK), the Frances and Augustus
Newman Foundation (TPJK) for financial support. The research leading to these results
has received funding from the European Research Council under the European Union's
Seventh Framework Programme (FP7/2007-2013) through the ERC grants PhysProt (agreement
no. 337969), MAMBA (agreement no. 340890) and NovoNordiskFonden (SL).
article_processing_charge: No
article_type: original
author:
- first_name: Alexander J.
full_name: Dear, Alexander J.
last_name: Dear
- first_name: Georg
full_name: Meisl, Georg
last_name: Meisl
- first_name: Anđela
full_name: Šarić, Anđela
id: bf63d406-f056-11eb-b41d-f263a6566d8b
last_name: Šarić
orcid: 0000-0002-7854-2139
- first_name: Thomas C. T.
full_name: Michaels, Thomas C. T.
last_name: Michaels
- first_name: Magnus
full_name: Kjaergaard, Magnus
last_name: Kjaergaard
- first_name: Sara
full_name: Linse, Sara
last_name: Linse
- first_name: Tuomas P. J.
full_name: Knowles, Tuomas P. J.
last_name: Knowles
citation:
ama: Dear AJ, Meisl G, Šarić A, et al. Identification of on- and off-pathway oligomers
in amyloid fibril formation. Chemical Science. 2020;11(24):6236-6247. doi:10.1039/c9sc06501f
apa: Dear, A. J., Meisl, G., Šarić, A., Michaels, T. C. T., Kjaergaard, M., Linse,
S., & Knowles, T. P. J. (2020). Identification of on- and off-pathway oligomers
in amyloid fibril formation. Chemical Science. Royal Society of Chemistry.
https://doi.org/10.1039/c9sc06501f
chicago: Dear, Alexander J., Georg Meisl, Anđela Šarić, Thomas C. T. Michaels, Magnus
Kjaergaard, Sara Linse, and Tuomas P. J. Knowles. “Identification of On- and off-Pathway
Oligomers in Amyloid Fibril Formation.” Chemical Science. Royal Society
of Chemistry, 2020. https://doi.org/10.1039/c9sc06501f.
ieee: A. J. Dear et al., “Identification of on- and off-pathway oligomers
in amyloid fibril formation,” Chemical Science, vol. 11, no. 24. Royal
Society of Chemistry, pp. 6236–6247, 2020.
ista: Dear AJ, Meisl G, Šarić A, Michaels TCT, Kjaergaard M, Linse S, Knowles TPJ.
2020. Identification of on- and off-pathway oligomers in amyloid fibril formation.
Chemical Science. 11(24), 6236–6247.
mla: Dear, Alexander J., et al. “Identification of On- and off-Pathway Oligomers
in Amyloid Fibril Formation.” Chemical Science, vol. 11, no. 24, Royal
Society of Chemistry, 2020, pp. 6236–47, doi:10.1039/c9sc06501f.
short: A.J. Dear, G. Meisl, A. Šarić, T.C.T. Michaels, M. Kjaergaard, S. Linse,
T.P.J. Knowles, Chemical Science 11 (2020) 6236–6247.
date_created: 2021-11-26T09:08:19Z
date_published: 2020-06-08T00:00:00Z
date_updated: 2021-11-26T11:21:20Z
day: '08'
doi: 10.1039/c9sc06501f
extern: '1'
external_id:
pmid:
- '32953019'
intvolume: ' 11'
issue: '24'
keyword:
- general chemistry
language:
- iso: eng
license: https://creativecommons.org/licenses/by-nc/3.0/
main_file_link:
- open_access: '1'
url: https://pubs.rsc.org/en/content/articlehtml/2020/sc/c9sc06501f
month: '06'
oa: 1
oa_version: Published Version
page: 6236-6247
pmid: 1
publication: Chemical Science
publication_identifier:
eissn:
- 2041-6539
issn:
- 2041-6520
publication_status: published
publisher: Royal Society of Chemistry
quality_controlled: '1'
scopus_import: '1'
status: public
title: Identification of on- and off-pathway oligomers in amyloid fibril formation
tmp:
image: /images/cc_by_nc.png
legal_code_url: https://creativecommons.org/licenses/by-nc/3.0/legalcode
name: Creative Commons Attribution-NonCommercial 3.0 Unported (CC BY-NC 3.0)
short: CC BY-NC (3.0)
type: journal_article
user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9
volume: 11
year: '2020'
...
---
_id: '10351'
abstract:
- lang: eng
text: Oligomeric species populated during the aggregation of the Aβ42 peptide have
been identified as potent cytotoxins linked to Alzheimer’s disease, but the fundamental
molecular pathways that control their dynamics have yet to be elucidated. By developing
a general approach that combines theory, experiment and simulation, we reveal,
in molecular detail, the mechanisms of Aβ42 oligomer dynamics during amyloid fibril
formation. Even though all mature amyloid fibrils must originate as oligomers,
we found that most Aβ42 oligomers dissociate into their monomeric precursors without
forming new fibrils. Only a minority of oligomers converts into fibrillar structures.
Moreover, the heterogeneous ensemble of oligomeric species interconverts on timescales
comparable to those of aggregation. Our results identify fundamentally new steps
that could be targeted by therapeutic interventions designed to combat protein
misfolding diseases.
acknowledgement: We acknowledge support from Peterhouse (T.C.T.M.), the Swiss National
Science foundation (T.C.T.M.), the Royal Society (A.Š.), the Academy of Medical
Sciences (A.Š.), the UCL Institute for the Physics of Living Systems (S.C.), Sidney
Sussex College (G.M.), the Wellcome Trust (A.Š., M.V., C.M.D. and T.P.J.K.), the
Schiff Foundation (A.J.D.), the Cambridge Centre for Misfolding Diseases (M.V.,
C.M.D. and T.P.J.K.), the BBSRC (C.M.D. and T.P.J.K.), the Frances and Augustus
Newman Foundation (T.P.J.K.), the Swedish Research Council (S.L.) and the ERC grant
MAMBA (S.L., agreement no. 340890). The research that led to these results received
funding from the European Research Council under the European Union’s Seventh Framework
Programme (FP7/2007-2013) through the ERC grant PhysProt (agreement no. 337969).
article_processing_charge: No
article_type: original
author:
- first_name: Thomas C. T.
full_name: Michaels, Thomas C. T.
last_name: Michaels
- first_name: Anđela
full_name: Šarić, Anđela
id: bf63d406-f056-11eb-b41d-f263a6566d8b
last_name: Šarić
orcid: 0000-0002-7854-2139
- first_name: Samo
full_name: Curk, Samo
last_name: Curk
- first_name: Katja
full_name: Bernfur, Katja
last_name: Bernfur
- first_name: Paolo
full_name: Arosio, Paolo
last_name: Arosio
- first_name: Georg
full_name: Meisl, Georg
last_name: Meisl
- first_name: Alexander J.
full_name: Dear, Alexander J.
last_name: Dear
- first_name: Samuel I. A.
full_name: Cohen, Samuel I. A.
last_name: Cohen
- first_name: Christopher M.
full_name: Dobson, Christopher M.
last_name: Dobson
- first_name: Michele
full_name: Vendruscolo, Michele
last_name: Vendruscolo
- first_name: Sara
full_name: Linse, Sara
last_name: Linse
- first_name: Tuomas P. J.
full_name: Knowles, Tuomas P. J.
last_name: Knowles
citation:
ama: Michaels TCT, Šarić A, Curk S, et al. Dynamics of oligomer populations formed
during the aggregation of Alzheimer’s Aβ42 peptide. Nature Chemistry. 2020;12(5):445-451.
doi:10.1038/s41557-020-0452-1
apa: Michaels, T. C. T., Šarić, A., Curk, S., Bernfur, K., Arosio, P., Meisl, G.,
… Knowles, T. P. J. (2020). Dynamics of oligomer populations formed during the
aggregation of Alzheimer’s Aβ42 peptide. Nature Chemistry. Springer Nature.
https://doi.org/10.1038/s41557-020-0452-1
chicago: Michaels, Thomas C. T., Anđela Šarić, Samo Curk, Katja Bernfur, Paolo Arosio,
Georg Meisl, Alexander J. Dear, et al. “Dynamics of Oligomer Populations Formed
during the Aggregation of Alzheimer’s Aβ42 Peptide.” Nature Chemistry.
Springer Nature, 2020. https://doi.org/10.1038/s41557-020-0452-1.
ieee: T. C. T. Michaels et al., “Dynamics of oligomer populations formed
during the aggregation of Alzheimer’s Aβ42 peptide,” Nature Chemistry,
vol. 12, no. 5. Springer Nature, pp. 445–451, 2020.
ista: Michaels TCT, Šarić A, Curk S, Bernfur K, Arosio P, Meisl G, Dear AJ, Cohen
SIA, Dobson CM, Vendruscolo M, Linse S, Knowles TPJ. 2020. Dynamics of oligomer
populations formed during the aggregation of Alzheimer’s Aβ42 peptide. Nature
Chemistry. 12(5), 445–451.
mla: Michaels, Thomas C. T., et al. “Dynamics of Oligomer Populations Formed during
the Aggregation of Alzheimer’s Aβ42 Peptide.” Nature Chemistry, vol. 12,
no. 5, Springer Nature, 2020, pp. 445–51, doi:10.1038/s41557-020-0452-1.
short: T.C.T. Michaels, A. Šarić, S. Curk, K. Bernfur, P. Arosio, G. Meisl, A.J.
Dear, S.I.A. Cohen, C.M. Dobson, M. Vendruscolo, S. Linse, T.P.J. Knowles, Nature
Chemistry 12 (2020) 445–451.
date_created: 2021-11-26T09:15:13Z
date_published: 2020-04-13T00:00:00Z
date_updated: 2021-11-26T11:21:08Z
day: '13'
doi: 10.1038/s41557-020-0452-1
extern: '1'
external_id:
pmid:
- '32303714'
intvolume: ' 12'
issue: '5'
keyword:
- general chemical engineering
- general chemistry
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://www.biorxiv.org/content/10.1101/2020.01.08.897488
month: '04'
oa: 1
oa_version: None
page: 445-451
pmid: 1
publication: Nature Chemistry
publication_identifier:
eissn:
- 1755-4349
issn:
- 1755-4330
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
related_material:
link:
- relation: erratum
url: https://doi.org/10.1038/s41557-020-0468-6
scopus_import: '1'
status: public
title: Dynamics of oligomer populations formed during the aggregation of Alzheimer’s
Aβ42 peptide
type: journal_article
user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9
volume: 12
year: '2020'
...
---
_id: '8405'
abstract:
- lang: eng
text: Atomic-resolution structure determination is crucial for understanding protein
function. Cryo-EM and NMR spectroscopy both provide structural information, but
currently cryo-EM does not routinely give access to atomic-level structural data,
and, generally, NMR structure determination is restricted to small (<30 kDa) proteins.
We introduce an integrated structure determination approach that simultaneously
uses NMR and EM data to overcome the limits of each of these methods. The approach
enables structure determination of the 468 kDa large dodecameric aminopeptidase
TET2 to a precision and accuracy below 1 Å by combining secondary-structure information
obtained from near-complete magic-angle-spinning NMR assignments of the 39 kDa-large
subunits, distance restraints from backbone amides and ILV methyl groups, and
a 4.1 Å resolution EM map. The resulting structure exceeds current standards of
NMR and EM structure determination in terms of molecular weight and precision.
Importantly, the approach is successful even in cases where only medium-resolution
cryo-EM data are available.
article_number: '2697'
article_processing_charge: No
article_type: original
author:
- first_name: Diego F.
full_name: Gauto, Diego F.
last_name: Gauto
- first_name: Leandro F.
full_name: Estrozi, Leandro F.
last_name: Estrozi
- first_name: Charles D.
full_name: Schwieters, Charles D.
last_name: Schwieters
- first_name: Gregory
full_name: Effantin, Gregory
last_name: Effantin
- first_name: Pavel
full_name: Macek, Pavel
last_name: Macek
- first_name: Remy
full_name: Sounier, Remy
last_name: Sounier
- first_name: Astrid C.
full_name: Sivertsen, Astrid C.
last_name: Sivertsen
- first_name: Elena
full_name: Schmidt, Elena
last_name: Schmidt
- first_name: Rime
full_name: Kerfah, Rime
last_name: Kerfah
- first_name: Guillaume
full_name: Mas, Guillaume
last_name: Mas
- first_name: Jacques-Philippe
full_name: Colletier, Jacques-Philippe
last_name: Colletier
- first_name: Peter
full_name: Güntert, Peter
last_name: Güntert
- first_name: Adrien
full_name: Favier, Adrien
last_name: Favier
- first_name: Guy
full_name: Schoehn, Guy
last_name: Schoehn
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
- first_name: Jerome
full_name: Boisbouvier, Jerome
last_name: Boisbouvier
citation:
ama: Gauto DF, Estrozi LF, Schwieters CD, et al. Integrated NMR and cryo-EM atomic-resolution
structure determination of a half-megadalton enzyme complex. Nature Communications.
2019;10. doi:10.1038/s41467-019-10490-9
apa: Gauto, D. F., Estrozi, L. F., Schwieters, C. D., Effantin, G., Macek, P., Sounier,
R., … Boisbouvier, J. (2019). Integrated NMR and cryo-EM atomic-resolution structure
determination of a half-megadalton enzyme complex. Nature Communications.
Springer Nature. https://doi.org/10.1038/s41467-019-10490-9
chicago: Gauto, Diego F., Leandro F. Estrozi, Charles D. Schwieters, Gregory Effantin,
Pavel Macek, Remy Sounier, Astrid C. Sivertsen, et al. “Integrated NMR and Cryo-EM
Atomic-Resolution Structure Determination of a Half-Megadalton Enzyme Complex.”
Nature Communications. Springer Nature, 2019. https://doi.org/10.1038/s41467-019-10490-9.
ieee: D. F. Gauto et al., “Integrated NMR and cryo-EM atomic-resolution structure
determination of a half-megadalton enzyme complex,” Nature Communications,
vol. 10. Springer Nature, 2019.
ista: Gauto DF, Estrozi LF, Schwieters CD, Effantin G, Macek P, Sounier R, Sivertsen
AC, Schmidt E, Kerfah R, Mas G, Colletier J-P, Güntert P, Favier A, Schoehn G,
Schanda P, Boisbouvier J. 2019. Integrated NMR and cryo-EM atomic-resolution structure
determination of a half-megadalton enzyme complex. Nature Communications. 10,
2697.
mla: Gauto, Diego F., et al. “Integrated NMR and Cryo-EM Atomic-Resolution Structure
Determination of a Half-Megadalton Enzyme Complex.” Nature Communications,
vol. 10, 2697, Springer Nature, 2019, doi:10.1038/s41467-019-10490-9.
short: D.F. Gauto, L.F. Estrozi, C.D. Schwieters, G. Effantin, P. Macek, R. Sounier,
A.C. Sivertsen, E. Schmidt, R. Kerfah, G. Mas, J.-P. Colletier, P. Güntert, A.
Favier, G. Schoehn, P. Schanda, J. Boisbouvier, Nature Communications 10 (2019).
date_created: 2020-09-17T10:28:25Z
date_published: 2019-06-19T00:00:00Z
date_updated: 2021-01-12T08:19:03Z
day: '19'
doi: 10.1038/s41467-019-10490-9
extern: '1'
external_id:
pmid:
- '31217444'
intvolume: ' 10'
keyword:
- General Biochemistry
- Genetics and Molecular Biology
- General Physics and Astronomy
- General Chemistry
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1038/s41467-019-10490-9
month: '06'
oa: 1
oa_version: Published Version
pmid: 1
publication: Nature Communications
publication_identifier:
issn:
- 2041-1723
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
status: public
title: Integrated NMR and cryo-EM atomic-resolution structure determination of a half-megadalton
enzyme complex
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 10
year: '2019'
...
---
_id: '8408'
abstract:
- lang: eng
text: Aromatic residues are located at structurally important sites of many proteins.
Probing their interactions and dynamics can provide important functional insight
but is challenging in large proteins. Here, we introduce approaches to characterize
dynamics of phenylalanine residues using 1H-detected fast magic-angle spinning
(MAS) NMR combined with a tailored isotope-labeling scheme. Our approach yields
isolated two-spin systems that are ideally suited for artefact-free dynamics measurements,
and allows probing motions effectively without molecular-weight limitations. The
application to the TET2 enzyme assembly of ~0.5 MDa size, the currently largest
protein assigned by MAS NMR, provides insights into motions occurring on a wide
range of time scales (ps-ms). We quantitatively probe ring flip motions, and show
the temperature dependence by MAS NMR measurements down to 100 K. Interestingly,
favorable line widths are observed down to 100 K, with potential implications
for DNP NMR. Furthermore, we report the first 13C R1ρ MAS NMR relaxation-dispersion
measurements and detect structural excursions occurring on a microsecond time
scale in the entry pore to the catalytic chamber and at a trimer interface that
was proposed as exit pore. We show that the labeling scheme with deuteration at
ca. 50 kHz MAS provides superior resolution compared to 100 kHz MAS experiments
with protonated, uniformly 13C-labeled samples.
article_processing_charge: No
article_type: original
author:
- first_name: Diego F.
full_name: Gauto, Diego F.
last_name: Gauto
- first_name: Pavel
full_name: Macek, Pavel
last_name: Macek
- first_name: Alessandro
full_name: Barducci, Alessandro
last_name: Barducci
- first_name: Hugo
full_name: Fraga, Hugo
last_name: Fraga
- first_name: Audrey
full_name: Hessel, Audrey
last_name: Hessel
- first_name: Tsutomu
full_name: Terauchi, Tsutomu
last_name: Terauchi
- first_name: David
full_name: Gajan, David
last_name: Gajan
- first_name: Yohei
full_name: Miyanoiri, Yohei
last_name: Miyanoiri
- first_name: Jerome
full_name: Boisbouvier, Jerome
last_name: Boisbouvier
- first_name: Roman
full_name: Lichtenecker, Roman
last_name: Lichtenecker
- first_name: Masatsune
full_name: Kainosho, Masatsune
last_name: Kainosho
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
citation:
ama: Gauto DF, Macek P, Barducci A, et al. Aromatic ring dynamics, thermal activation,
and transient conformations of a 468 kDa enzyme by specific 1H–13C labeling and
fast magic-angle spinning NMR. Journal of the American Chemical Society.
2019;141(28):11183-11195. doi:10.1021/jacs.9b04219
apa: Gauto, D. F., Macek, P., Barducci, A., Fraga, H., Hessel, A., Terauchi, T.,
… Schanda, P. (2019). Aromatic ring dynamics, thermal activation, and transient
conformations of a 468 kDa enzyme by specific 1H–13C labeling and fast magic-angle
spinning NMR. Journal of the American Chemical Society. American Chemical
Society. https://doi.org/10.1021/jacs.9b04219
chicago: Gauto, Diego F., Pavel Macek, Alessandro Barducci, Hugo Fraga, Audrey Hessel,
Tsutomu Terauchi, David Gajan, et al. “Aromatic Ring Dynamics, Thermal Activation,
and Transient Conformations of a 468 KDa Enzyme by Specific 1H–13C Labeling and
Fast Magic-Angle Spinning NMR.” Journal of the American Chemical Society.
American Chemical Society, 2019. https://doi.org/10.1021/jacs.9b04219.
ieee: D. F. Gauto et al., “Aromatic ring dynamics, thermal activation, and
transient conformations of a 468 kDa enzyme by specific 1H–13C labeling and fast
magic-angle spinning NMR,” Journal of the American Chemical Society, vol.
141, no. 28. American Chemical Society, pp. 11183–11195, 2019.
ista: Gauto DF, Macek P, Barducci A, Fraga H, Hessel A, Terauchi T, Gajan D, Miyanoiri
Y, Boisbouvier J, Lichtenecker R, Kainosho M, Schanda P. 2019. Aromatic ring dynamics,
thermal activation, and transient conformations of a 468 kDa enzyme by specific
1H–13C labeling and fast magic-angle spinning NMR. Journal of the American Chemical
Society. 141(28), 11183–11195.
mla: Gauto, Diego F., et al. “Aromatic Ring Dynamics, Thermal Activation, and Transient
Conformations of a 468 KDa Enzyme by Specific 1H–13C Labeling and Fast Magic-Angle
Spinning NMR.” Journal of the American Chemical Society, vol. 141, no.
28, American Chemical Society, 2019, pp. 11183–95, doi:10.1021/jacs.9b04219.
short: D.F. Gauto, P. Macek, A. Barducci, H. Fraga, A. Hessel, T. Terauchi, D. Gajan,
Y. Miyanoiri, J. Boisbouvier, R. Lichtenecker, M. Kainosho, P. Schanda, Journal
of the American Chemical Society 141 (2019) 11183–11195.
date_created: 2020-09-17T10:29:00Z
date_published: 2019-06-14T00:00:00Z
date_updated: 2021-01-12T08:19:04Z
day: '14'
doi: 10.1021/jacs.9b04219
extern: '1'
external_id:
pmid:
- '31199882'
intvolume: ' 141'
issue: '28'
keyword:
- Colloid and Surface Chemistry
- Biochemistry
- General Chemistry
- Catalysis
language:
- iso: eng
month: '06'
oa_version: Submitted Version
page: 11183-11195
pmid: 1
publication: Journal of the American Chemical Society
publication_identifier:
issn:
- 0002-7863
- 1520-5126
publication_status: published
publisher: American Chemical Society
quality_controlled: '1'
status: public
title: Aromatic ring dynamics, thermal activation, and transient conformations of
a 468 kDa enzyme by specific 1H–13C labeling and fast magic-angle spinning NMR
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 141
year: '2019'
...
---
_id: '8413'
abstract:
- lang: eng
text: NMR relaxation dispersion methods provide a holistic way to observe microsecond
time-scale protein backbone motion both in solution and in the solid state. Different
nuclei (1H and 15N) and different relaxation dispersion techniques (Bloch–McConnell
and near-rotary-resonance) give complementary information about the amplitudes
and time scales of the conformational dynamics and provide comprehensive insights
into the mechanistic details of the structural rearrangements. In this paper,
we exemplify the benefits of the combination of various solution- and solid-state
relaxation dispersion methods on a microcrystalline protein (α-spectrin SH3 domain),
for which we are able to identify and model the functionally relevant conformational
rearrangements around the ligand recognition loop occurring on multiple microsecond
time scales. The observed loop motions suggest that the SH3 domain exists in a
binding-competent conformation in dynamic equilibrium with a sterically impaired
ground-state conformation both in solution and in crystalline form. This inherent
plasticity between the interconverting macrostates is compatible with a conformational-preselection
model and provides new insights into the recognition mechanisms of SH3 domains.
article_processing_charge: No
article_type: original
author:
- first_name: Petra
full_name: Rovó, Petra
last_name: Rovó
- first_name: Colin A.
full_name: Smith, Colin A.
last_name: Smith
- first_name: Diego
full_name: Gauto, Diego
last_name: Gauto
- first_name: Bert L.
full_name: de Groot, Bert L.
last_name: de Groot
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
- first_name: Rasmus
full_name: Linser, Rasmus
last_name: Linser
citation:
ama: Rovó P, Smith CA, Gauto D, de Groot BL, Schanda P, Linser R. Mechanistic insights
into microsecond time-scale motion of solid proteins using complementary 15N and
1H relaxation dispersion techniques. Journal of the American Chemical Society.
2019;141(2):858-869. doi:10.1021/jacs.8b09258
apa: Rovó, P., Smith, C. A., Gauto, D., de Groot, B. L., Schanda, P., & Linser,
R. (2019). Mechanistic insights into microsecond time-scale motion of solid proteins
using complementary 15N and 1H relaxation dispersion techniques. Journal of
the American Chemical Society. American Chemical Society. https://doi.org/10.1021/jacs.8b09258
chicago: Rovó, Petra, Colin A. Smith, Diego Gauto, Bert L. de Groot, Paul Schanda,
and Rasmus Linser. “Mechanistic Insights into Microsecond Time-Scale Motion of
Solid Proteins Using Complementary 15N and 1H Relaxation Dispersion Techniques.”
Journal of the American Chemical Society. American Chemical Society, 2019.
https://doi.org/10.1021/jacs.8b09258.
ieee: P. Rovó, C. A. Smith, D. Gauto, B. L. de Groot, P. Schanda, and R. Linser,
“Mechanistic insights into microsecond time-scale motion of solid proteins using
complementary 15N and 1H relaxation dispersion techniques,” Journal of the
American Chemical Society, vol. 141, no. 2. American Chemical Society, pp.
858–869, 2019.
ista: Rovó P, Smith CA, Gauto D, de Groot BL, Schanda P, Linser R. 2019. Mechanistic
insights into microsecond time-scale motion of solid proteins using complementary
15N and 1H relaxation dispersion techniques. Journal of the American Chemical
Society. 141(2), 858–869.
mla: Rovó, Petra, et al. “Mechanistic Insights into Microsecond Time-Scale Motion
of Solid Proteins Using Complementary 15N and 1H Relaxation Dispersion Techniques.”
Journal of the American Chemical Society, vol. 141, no. 2, American Chemical
Society, 2019, pp. 858–69, doi:10.1021/jacs.8b09258.
short: P. Rovó, C.A. Smith, D. Gauto, B.L. de Groot, P. Schanda, R. Linser, Journal
of the American Chemical Society 141 (2019) 858–869.
date_created: 2020-09-17T10:29:50Z
date_published: 2019-01-08T00:00:00Z
date_updated: 2021-01-12T08:19:07Z
day: '08'
doi: 10.1021/jacs.8b09258
extern: '1'
external_id:
pmid:
- '30620186'
intvolume: ' 141'
issue: '2'
keyword:
- Colloid and Surface Chemistry
- Biochemistry
- General Chemistry
- Catalysis
language:
- iso: eng
month: '01'
oa_version: Submitted Version
page: 858-869
pmid: 1
publication: Journal of the American Chemical Society
publication_identifier:
issn:
- 0002-7863
- 1520-5126
publication_status: published
publisher: American Chemical Society
quality_controlled: '1'
status: public
title: Mechanistic insights into microsecond time-scale motion of solid proteins using
complementary 15N and 1H relaxation dispersion techniques
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 141
year: '2019'
...
---
_id: '13370'
abstract:
- lang: eng
text: Efficient isomerization of photochromic molecules often requires conformational
freedom and is typically not available under solvent-free conditions. Here, we
report a general methodology allowing for reversible switching of such molecules
on the surfaces of solid materials. Our method is based on dispersing photochromic
compounds within polysilsesquioxane nanowire networks (PNNs), which can be fabricated
as transparent, highly porous, micrometer-thick layers on various substrates.
We found that azobenzene switching within the PNNs proceeded unusually fast compared
with the same molecules in liquid solvents. Efficient isomerization of another
photochromic system, spiropyran, from a colorless to a colored form was used to
create reversible images in PNN-coated glass. The coloration reaction could be
induced with sunlight and is of interest for developing “smart” windows.
article_processing_charge: No
article_type: original
author:
- first_name: Zonglin
full_name: Chu, Zonglin
last_name: Chu
- first_name: Rafal
full_name: Klajn, Rafal
id: 8e84690e-1e48-11ed-a02b-a1e6fb8bb53b
last_name: Klajn
citation:
ama: Chu Z, Klajn R. Polysilsesquioxane nanowire networks as an “Artificial Solvent”
for reversible operation of photochromic molecules. Nano Letters. 2019;19(10):7106-7111.
doi:10.1021/acs.nanolett.9b02642
apa: Chu, Z., & Klajn, R. (2019). Polysilsesquioxane nanowire networks as an
“Artificial Solvent” for reversible operation of photochromic molecules. Nano
Letters. American Chemical Society. https://doi.org/10.1021/acs.nanolett.9b02642
chicago: Chu, Zonglin, and Rafal Klajn. “Polysilsesquioxane Nanowire Networks as
an ‘Artificial Solvent’ for Reversible Operation of Photochromic Molecules.” Nano
Letters. American Chemical Society, 2019. https://doi.org/10.1021/acs.nanolett.9b02642.
ieee: Z. Chu and R. Klajn, “Polysilsesquioxane nanowire networks as an ‘Artificial
Solvent’ for reversible operation of photochromic molecules,” Nano Letters,
vol. 19, no. 10. American Chemical Society, pp. 7106–7111, 2019.
ista: Chu Z, Klajn R. 2019. Polysilsesquioxane nanowire networks as an “Artificial
Solvent” for reversible operation of photochromic molecules. Nano Letters. 19(10),
7106–7111.
mla: Chu, Zonglin, and Rafal Klajn. “Polysilsesquioxane Nanowire Networks as an
‘Artificial Solvent’ for Reversible Operation of Photochromic Molecules.” Nano
Letters, vol. 19, no. 10, American Chemical Society, 2019, pp. 7106–11, doi:10.1021/acs.nanolett.9b02642.
short: Z. Chu, R. Klajn, Nano Letters 19 (2019) 7106–7111.
date_created: 2023-08-01T09:38:23Z
date_published: 2019-09-20T00:00:00Z
date_updated: 2023-08-07T10:39:34Z
day: '20'
doi: 10.1021/acs.nanolett.9b02642
extern: '1'
external_id:
pmid:
- '31539469'
intvolume: ' 19'
issue: '10'
keyword:
- Mechanical Engineering
- Condensed Matter Physics
- General Materials Science
- General Chemistry
- Bioengineering
language:
- iso: eng
month: '09'
oa_version: None
page: 7106-7111
pmid: 1
publication: Nano Letters
publication_identifier:
eissn:
- 1530-6992
issn:
- 1530-6984
publication_status: published
publisher: American Chemical Society
quality_controlled: '1'
scopus_import: '1'
status: public
title: Polysilsesquioxane nanowire networks as an “Artificial Solvent” for reversible
operation of photochromic molecules
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 19
year: '2019'
...
---
_id: '13371'
abstract:
- lang: eng
text: Diamondoid nanoporous crystals represent a synthetically challenging class
of materials that typically have been obtained from tetrahedral building blocks.
In this issue of Chem, Stoddart and coworkers demonstrate that it is possible
to generate diamondoid frameworks from a hexacationic building block lacking a
tetrahedral symmetry. These results highlight the great potential of self-assembly
for rapidly transforming small molecules into structurally complex functional
materials.
article_processing_charge: No
article_type: original
author:
- first_name: Michał J.
full_name: Białek, Michał J.
last_name: Białek
- first_name: Rafal
full_name: Klajn, Rafal
id: 8e84690e-1e48-11ed-a02b-a1e6fb8bb53b
last_name: Klajn
citation:
ama: Białek MJ, Klajn R. Diamond grows up. Chem. 2019;5(9):2283-2285. doi:10.1016/j.chempr.2019.08.012
apa: Białek, M. J., & Klajn, R. (2019). Diamond grows up. Chem. Elsevier.
https://doi.org/10.1016/j.chempr.2019.08.012
chicago: Białek, Michał J., and Rafal Klajn. “Diamond Grows Up.” Chem. Elsevier,
2019. https://doi.org/10.1016/j.chempr.2019.08.012.
ieee: M. J. Białek and R. Klajn, “Diamond grows up,” Chem, vol. 5, no. 9.
Elsevier, pp. 2283–2285, 2019.
ista: Białek MJ, Klajn R. 2019. Diamond grows up. Chem. 5(9), 2283–2285.
mla: Białek, Michał J., and Rafal Klajn. “Diamond Grows Up.” Chem, vol. 5,
no. 9, Elsevier, 2019, pp. 2283–85, doi:10.1016/j.chempr.2019.08.012.
short: M.J. Białek, R. Klajn, Chem 5 (2019) 2283–2285.
date_created: 2023-08-01T09:38:38Z
date_published: 2019-09-12T00:00:00Z
date_updated: 2023-08-07T10:46:50Z
day: '12'
doi: 10.1016/j.chempr.2019.08.012
extern: '1'
intvolume: ' 5'
issue: '9'
keyword:
- Materials Chemistry
- Biochemistry (medical)
- General Chemical Engineering
- Environmental Chemistry
- Biochemistry
- General Chemistry
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1016/j.chempr.2019.08.012
month: '09'
oa: 1
oa_version: Published Version
page: 2283-2285
publication: Chem
publication_identifier:
eissn:
- 2451-9294
issn:
- 2451-9308
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: Diamond grows up
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 5
year: '2019'
...
---
_id: '13372'
abstract:
- lang: eng
text: 'The capacity to respond or adapt to environmental changes is an intrinsic
property of living systems that comprise highly-connected subcomponents communicating
through chemical networks. The development of responsive synthetic systems is
a relatively new research area that covers different disciplines, among which
nanochemistry brings conceptually new demonstrations. Especially attractive are
ligand-protected gold nanoparticles, which have been extensively used over the
last decade as building blocks in constructing superlattices or dynamic aggregates,
under the effect of an applied stimulus. To reflect the importance of surface
chemistry and nanoparticle core composition in the dynamic self-assembly of nanoparticles,
we provide here an overview of various available stimuli, as tools for synthetic
chemists to exploit. Along with this task, the review starts with the use of chemical
stimuli such as solvent, pH, gases, metal ions or biomolecules. It then focuses
on physical stimuli: temperature, magnetic and electric fields, as well as light.
To reflect on the increasing complexity of current architectures, we discuss systems
that are responsive to more than one stimulus, to finally encourage further research
by proposing future challenges.'
article_processing_charge: No
article_type: original
author:
- first_name: Marek
full_name: Grzelczak, Marek
last_name: Grzelczak
- first_name: Luis M.
full_name: Liz-Marzán, Luis M.
last_name: Liz-Marzán
- first_name: Rafal
full_name: Klajn, Rafal
id: 8e84690e-1e48-11ed-a02b-a1e6fb8bb53b
last_name: Klajn
citation:
ama: Grzelczak M, Liz-Marzán LM, Klajn R. Stimuli-responsive self-assembly of nanoparticles.
Chemical Society Reviews. 2019;48(5):1342-1361. doi:10.1039/c8cs00787j
apa: Grzelczak, M., Liz-Marzán, L. M., & Klajn, R. (2019). Stimuli-responsive
self-assembly of nanoparticles. Chemical Society Reviews. Royal Society
of Chemistry. https://doi.org/10.1039/c8cs00787j
chicago: Grzelczak, Marek, Luis M. Liz-Marzán, and Rafal Klajn. “Stimuli-Responsive
Self-Assembly of Nanoparticles.” Chemical Society Reviews. Royal Society
of Chemistry, 2019. https://doi.org/10.1039/c8cs00787j.
ieee: M. Grzelczak, L. M. Liz-Marzán, and R. Klajn, “Stimuli-responsive self-assembly
of nanoparticles,” Chemical Society Reviews, vol. 48, no. 5. Royal Society
of Chemistry, pp. 1342–1361, 2019.
ista: Grzelczak M, Liz-Marzán LM, Klajn R. 2019. Stimuli-responsive self-assembly
of nanoparticles. Chemical Society Reviews. 48(5), 1342–1361.
mla: Grzelczak, Marek, et al. “Stimuli-Responsive Self-Assembly of Nanoparticles.”
Chemical Society Reviews, vol. 48, no. 5, Royal Society of Chemistry, 2019,
pp. 1342–61, doi:10.1039/c8cs00787j.
short: M. Grzelczak, L.M. Liz-Marzán, R. Klajn, Chemical Society Reviews 48 (2019)
1342–1361.
date_created: 2023-08-01T09:38:52Z
date_published: 2019-01-28T00:00:00Z
date_updated: 2023-08-07T10:48:31Z
day: '28'
doi: 10.1039/c8cs00787j
extern: '1'
external_id:
pmid:
- '30688963'
intvolume: ' 48'
issue: '5'
keyword:
- General Chemistry
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1039/C8CS00787J
month: '01'
oa: 1
oa_version: Published Version
page: 1342-1361
pmid: 1
publication: Chemical Society Reviews
publication_identifier:
eissn:
- 1460-4744
issn:
- 0306-0012
publication_status: published
publisher: Royal Society of Chemistry
quality_controlled: '1'
scopus_import: '1'
status: public
title: Stimuli-responsive self-assembly of nanoparticles
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 48
year: '2019'
...
---
_id: '13373'
abstract:
- lang: eng
text: The reversible photoisomerization of azobenzene has been utilized to construct
a plethora of systems in which optical, electronic, catalytic, and other properties
can be controlled by light. However, owing to azobenzene’s hydrophobic nature,
most of these examples have been realized only in organic solvents, and systems
operating in water are relatively scarce. Here, we show that by coadsorbing the
inherently hydrophobic azobenzenes with water-solubilizing ligands on the same
nanoparticulate platforms, it is possible to render them essentially water-soluble.
To this end, we developed a modified nanoparticle functionalization procedure
allowing us to precisely fine-tune the amount of azobenzene on the functionalized
nanoparticles. Molecular dynamics simulations helped us to identify two distinct
supramolecular architectures (depending on the length of the background ligand)
on these nanoparticles, which can explain their excellent aqueous solubilities.
Azobenzenes adsorbed on these water-soluble nanoparticles exhibit highly reversible
photoisomerization upon exposure to UV and visible light. Importantly, the mixed-monolayer
approach allowed us to systematically investigate how the background ligand affects
the switching properties of azobenzene. We found that the nature of the background
ligand has a profound effect on the kinetics of azobenzene switching. For example,
a hydroxy-terminated background ligand is capable of accelerating the back-isomerization
reaction by more than 6000-fold. These results pave the way toward the development
of novel light-responsive nanomaterials operating in aqueous media and, in the
long run, in biological environments.
article_processing_charge: No
article_type: original
author:
- first_name: Zonglin
full_name: Chu, Zonglin
last_name: Chu
- first_name: Yanxiao
full_name: Han, Yanxiao
last_name: Han
- first_name: Tong
full_name: Bian, Tong
last_name: Bian
- first_name: Soumen
full_name: De, Soumen
last_name: De
- first_name: Petr
full_name: Král, Petr
last_name: Král
- first_name: Rafal
full_name: Klajn, Rafal
id: 8e84690e-1e48-11ed-a02b-a1e6fb8bb53b
last_name: Klajn
citation:
ama: Chu Z, Han Y, Bian T, De S, Král P, Klajn R. Supramolecular control of azobenzene
switching on nanoparticles. Journal of the American Chemical Society. 2019;141(5):1949-1960.
doi:10.1021/jacs.8b09638
apa: Chu, Z., Han, Y., Bian, T., De, S., Král, P., & Klajn, R. (2019). Supramolecular
control of azobenzene switching on nanoparticles. Journal of the American Chemical
Society. American Chemical Society. https://doi.org/10.1021/jacs.8b09638
chicago: Chu, Zonglin, Yanxiao Han, Tong Bian, Soumen De, Petr Král, and Rafal Klajn.
“Supramolecular Control of Azobenzene Switching on Nanoparticles.” Journal
of the American Chemical Society. American Chemical Society, 2019. https://doi.org/10.1021/jacs.8b09638.
ieee: Z. Chu, Y. Han, T. Bian, S. De, P. Král, and R. Klajn, “Supramolecular control
of azobenzene switching on nanoparticles,” Journal of the American Chemical
Society, vol. 141, no. 5. American Chemical Society, pp. 1949–1960, 2019.
ista: Chu Z, Han Y, Bian T, De S, Král P, Klajn R. 2019. Supramolecular control
of azobenzene switching on nanoparticles. Journal of the American Chemical Society.
141(5), 1949–1960.
mla: Chu, Zonglin, et al. “Supramolecular Control of Azobenzene Switching on Nanoparticles.”
Journal of the American Chemical Society, vol. 141, no. 5, American Chemical
Society, 2019, pp. 1949–60, doi:10.1021/jacs.8b09638.
short: Z. Chu, Y. Han, T. Bian, S. De, P. Král, R. Klajn, Journal of the American
Chemical Society 141 (2019) 1949–1960.
date_created: 2023-08-01T09:39:19Z
date_published: 2019-02-06T00:00:00Z
date_updated: 2023-08-07T10:51:12Z
day: '06'
doi: 10.1021/jacs.8b09638
extern: '1'
external_id:
pmid:
- '30595017'
intvolume: ' 141'
issue: '5'
keyword:
- Colloid and Surface Chemistry
- Biochemistry
- General Chemistry
- Catalysis
language:
- iso: eng
month: '02'
oa_version: Published Version
page: 1949-1960
pmid: 1
publication: Journal of the American Chemical Society
publication_identifier:
eissn:
- 1520-5126
issn:
- 0002-7863
publication_status: published
publisher: American Chemical Society
quality_controlled: '1'
scopus_import: '1'
status: public
title: Supramolecular control of azobenzene switching on nanoparticles
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 141
year: '2019'
...
---
_id: '9060'
abstract:
- lang: eng
text: Molecular motors are essential to the living, generating fluctuations that
boost transport and assist assembly. Active colloids, that consume energy to move,
hold similar potential for man-made materials controlled by forces generated from
within. Yet, their use as a powerhouse in materials science lacks. Here we show
a massive acceleration of the annealing of a monolayer of passive beads by moderate
addition of self-propelled microparticles. We rationalize our observations with
a model of collisions that drive active fluctuations and activate the annealing.
The experiment is quantitatively compared with Brownian dynamic simulations that
further unveil a dynamical transition in the mechanism of annealing. Active dopants
travel uniformly in the system or co-localize at the grain boundaries as a result
of the persistence of their motion. Our findings uncover the potential of internal
activity to control materials and lay the groundwork for the rise of materials
science beyond equilibrium.
article_number: '3380'
article_processing_charge: No
article_type: original
arxiv: 1
author:
- first_name: Sophie
full_name: Ramananarivo, Sophie
last_name: Ramananarivo
- first_name: Etienne
full_name: Ducrot, Etienne
last_name: Ducrot
- first_name: Jérémie A
full_name: Palacci, Jérémie A
id: 8fb92548-2b22-11eb-b7c1-a3f0d08d7c7d
last_name: Palacci
orcid: 0000-0002-7253-9465
citation:
ama: Ramananarivo S, Ducrot E, Palacci JA. Activity-controlled annealing of colloidal
monolayers. Nature Communications. 2019;10(1). doi:10.1038/s41467-019-11362-y
apa: Ramananarivo, S., Ducrot, E., & Palacci, J. A. (2019). Activity-controlled
annealing of colloidal monolayers. Nature Communications. Springer Nature.
https://doi.org/10.1038/s41467-019-11362-y
chicago: Ramananarivo, Sophie, Etienne Ducrot, and Jérémie A Palacci. “Activity-Controlled
Annealing of Colloidal Monolayers.” Nature Communications. Springer Nature,
2019. https://doi.org/10.1038/s41467-019-11362-y.
ieee: S. Ramananarivo, E. Ducrot, and J. A. Palacci, “Activity-controlled annealing
of colloidal monolayers,” Nature Communications, vol. 10, no. 1. Springer
Nature, 2019.
ista: Ramananarivo S, Ducrot E, Palacci JA. 2019. Activity-controlled annealing
of colloidal monolayers. Nature Communications. 10(1), 3380.
mla: Ramananarivo, Sophie, et al. “Activity-Controlled Annealing of Colloidal Monolayers.”
Nature Communications, vol. 10, no. 1, 3380, Springer Nature, 2019, doi:10.1038/s41467-019-11362-y.
short: S. Ramananarivo, E. Ducrot, J.A. Palacci, Nature Communications 10 (2019).
date_created: 2021-02-02T13:43:36Z
date_published: 2019-07-29T00:00:00Z
date_updated: 2023-02-23T13:47:59Z
day: '29'
ddc:
- '530'
doi: 10.1038/s41467-019-11362-y
extern: '1'
external_id:
arxiv:
- '1909.07382'
pmid:
- '31358762'
file:
- access_level: open_access
checksum: 70c6e5d6fbea0932b0669505ab6633ec
content_type: application/pdf
creator: cziletti
date_created: 2021-02-02T13:47:21Z
date_updated: 2021-02-02T13:47:21Z
file_id: '9061'
file_name: 2019_NatureComm_Ramananarivo.pdf
file_size: 2820337
relation: main_file
success: 1
file_date_updated: 2021-02-02T13:47:21Z
has_accepted_license: '1'
intvolume: ' 10'
issue: '1'
keyword:
- General Biochemistry
- Genetics and Molecular Biology
- General Physics and Astronomy
- General Chemistry
language:
- iso: eng
month: '07'
oa: 1
oa_version: Published Version
pmid: 1
publication: Nature Communications
publication_identifier:
issn:
- 2041-1723
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
scopus_import: '1'
status: public
title: Activity-controlled annealing of colloidal monolayers
tmp:
image: /images/cc_by.png
legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
short: CC BY (4.0)
type: journal_article
user_id: D865714E-FA4E-11E9-B85B-F5C5E5697425
volume: 10
year: '2019'
...
---
_id: '10622'
abstract:
- lang: eng
text: We demonstrate a method for manipulating small ensembles of vortices in multiply
connected superconducting structures. A micron-size magnetic particle attached
to the tip of a silicon cantilever is used to locally apply magnetic flux through
the superconducting structure. By scanning the tip over the surface of the device
and by utilizing the dynamical coupling between the vortices and the cantilever,
a high-resolution spatial map of the different vortex configurations is obtained.
Moving the tip to a particular location in the map stabilizes a distinct multivortex
configuration. Thus, the scanning of the tip over a particular trajectory in space
permits nontrivial operations to be performed, such as braiding of individual
vortices within a larger vortex ensemble—a key capability required by many proposals
for topological quantum computing.
acknowledgement: We are grateful to Nadya Mason, Taylor Hughes, and Alexey Bezryadin
for useful discussions. This work was supported by the DOE Basic Energy Sciences
under DE-SC0012649 and the Department of Physics and the Frederick Seitz Materials
Research Laboratory Central Facilities at the University of Illinois.
article_processing_charge: No
article_type: original
arxiv: 1
author:
- first_name: Hryhoriy
full_name: Polshyn, Hryhoriy
id: edfc7cb1-526e-11ec-b05a-e6ecc27e4e48
last_name: Polshyn
orcid: 0000-0001-8223-8896
- first_name: Tyler
full_name: Naibert, Tyler
last_name: Naibert
- first_name: Raffi
full_name: Budakian, Raffi
last_name: Budakian
citation:
ama: Polshyn H, Naibert T, Budakian R. Manipulating multivortex states in superconducting
structures. Nano Letters. 2019;19(8):5476-5482. doi:10.1021/acs.nanolett.9b01983
apa: Polshyn, H., Naibert, T., & Budakian, R. (2019). Manipulating multivortex
states in superconducting structures. Nano Letters. American Chemical Society.
https://doi.org/10.1021/acs.nanolett.9b01983
chicago: Polshyn, Hryhoriy, Tyler Naibert, and Raffi Budakian. “Manipulating Multivortex
States in Superconducting Structures.” Nano Letters. American Chemical
Society, 2019. https://doi.org/10.1021/acs.nanolett.9b01983.
ieee: H. Polshyn, T. Naibert, and R. Budakian, “Manipulating multivortex states
in superconducting structures,” Nano Letters, vol. 19, no. 8. American
Chemical Society, pp. 5476–5482, 2019.
ista: Polshyn H, Naibert T, Budakian R. 2019. Manipulating multivortex states in
superconducting structures. Nano Letters. 19(8), 5476–5482.
mla: Polshyn, Hryhoriy, et al. “Manipulating Multivortex States in Superconducting
Structures.” Nano Letters, vol. 19, no. 8, American Chemical Society, 2019,
pp. 5476–82, doi:10.1021/acs.nanolett.9b01983.
short: H. Polshyn, T. Naibert, R. Budakian, Nano Letters 19 (2019) 5476–5482.
date_created: 2022-01-13T15:11:14Z
date_published: 2019-06-27T00:00:00Z
date_updated: 2022-01-13T15:41:24Z
day: '27'
doi: 10.1021/acs.nanolett.9b01983
extern: '1'
external_id:
arxiv:
- '1905.06303'
pmid:
- '31246034'
intvolume: ' 19'
issue: '8'
keyword:
- mechanical engineering
- condensed matter physics
- general materials science
- general chemistry
- bioengineering
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://arxiv.org/abs/1905.06303
month: '06'
oa: 1
oa_version: Preprint
page: 5476-5482
pmid: 1
publication: Nano Letters
publication_identifier:
eissn:
- 1530-6992
issn:
- 1530-6984
publication_status: published
publisher: American Chemical Society
quality_controlled: '1'
scopus_import: '1'
status: public
title: Manipulating multivortex states in superconducting structures
type: journal_article
user_id: ea97e931-d5af-11eb-85d4-e6957dddbf17
volume: 19
year: '2019'
...