---
_id: '13357'
abstract:
- lang: eng
  text: Coulombic interactions can be used to assemble charged nanoparticles into
    higher-order structures, but the process requires oppositely charged partners
    that are similarly sized. The ability to mediate the assembly of such charged
    nanoparticles using structurally simple small molecules would greatly facilitate
    the fabrication of nanostructured materials and harnessing their applications
    in catalysis, sensing and photonics. Here we show that small molecules with as
    few as three electric charges can effectively induce attractive interactions between
    oppositely charged nanoparticles in water. These interactions can guide the assembly
    of charged nanoparticles into colloidal crystals of a quality previously only
    thought to result from their co-crystallization with oppositely charged nanoparticles
    of a similar size. Transient nanoparticle assemblies can be generated using positively
    charged nanoparticles and multiply charged anions that are enzymatically hydrolysed
    into mono- and/or dianions. Our findings demonstrate an approach for the facile
    fabrication, manipulation and further investigation of static and dynamic nanostructured
    materials in aqueous environments.
article_processing_charge: No
article_type: original
author:
- first_name: Tong
  full_name: Bian, Tong
  last_name: Bian
- first_name: Andrea
  full_name: Gardin, Andrea
  last_name: Gardin
- first_name: Julius
  full_name: Gemen, Julius
  last_name: Gemen
- first_name: Lothar
  full_name: Houben, Lothar
  last_name: Houben
- first_name: Claudio
  full_name: Perego, Claudio
  last_name: Perego
- first_name: Byeongdu
  full_name: Lee, Byeongdu
  last_name: Lee
- first_name: Nadav
  full_name: Elad, Nadav
  last_name: Elad
- first_name: Zonglin
  full_name: Chu, Zonglin
  last_name: Chu
- first_name: Giovanni M.
  full_name: Pavan, Giovanni M.
  last_name: Pavan
- first_name: Rafal
  full_name: Klajn, Rafal
  id: 8e84690e-1e48-11ed-a02b-a1e6fb8bb53b
  last_name: Klajn
citation:
  ama: Bian T, Gardin A, Gemen J, et al. Electrostatic co-assembly of nanoparticles
    with oppositely charged small molecules into static and dynamic superstructures.
    <i>Nature Chemistry</i>. 2021;13(10):940-949. doi:<a href="https://doi.org/10.1038/s41557-021-00752-9">10.1038/s41557-021-00752-9</a>
  apa: Bian, T., Gardin, A., Gemen, J., Houben, L., Perego, C., Lee, B., … Klajn,
    R. (2021). Electrostatic co-assembly of nanoparticles with oppositely charged
    small molecules into static and dynamic superstructures. <i>Nature Chemistry</i>.
    Springer Nature. <a href="https://doi.org/10.1038/s41557-021-00752-9">https://doi.org/10.1038/s41557-021-00752-9</a>
  chicago: Bian, Tong, Andrea Gardin, Julius Gemen, Lothar Houben, Claudio Perego,
    Byeongdu Lee, Nadav Elad, Zonglin Chu, Giovanni M. Pavan, and Rafal Klajn. “Electrostatic
    Co-Assembly of Nanoparticles with Oppositely Charged Small Molecules into Static
    and Dynamic Superstructures.” <i>Nature Chemistry</i>. Springer Nature, 2021.
    <a href="https://doi.org/10.1038/s41557-021-00752-9">https://doi.org/10.1038/s41557-021-00752-9</a>.
  ieee: T. Bian <i>et al.</i>, “Electrostatic co-assembly of nanoparticles with oppositely
    charged small molecules into static and dynamic superstructures,” <i>Nature Chemistry</i>,
    vol. 13, no. 10. Springer Nature, pp. 940–949, 2021.
  ista: Bian T, Gardin A, Gemen J, Houben L, Perego C, Lee B, Elad N, Chu Z, Pavan
    GM, Klajn R. 2021. Electrostatic co-assembly of nanoparticles with oppositely
    charged small molecules into static and dynamic superstructures. Nature Chemistry.
    13(10), 940–949.
  mla: Bian, Tong, et al. “Electrostatic Co-Assembly of Nanoparticles with Oppositely
    Charged Small Molecules into Static and Dynamic Superstructures.” <i>Nature Chemistry</i>,
    vol. 13, no. 10, Springer Nature, 2021, pp. 940–49, doi:<a href="https://doi.org/10.1038/s41557-021-00752-9">10.1038/s41557-021-00752-9</a>.
  short: T. Bian, A. Gardin, J. Gemen, L. Houben, C. Perego, B. Lee, N. Elad, Z. Chu,
    G.M. Pavan, R. Klajn, Nature Chemistry 13 (2021) 940–949.
date_created: 2023-08-01T09:34:54Z
date_published: 2021-10-01T00:00:00Z
date_updated: 2023-08-02T10:55:29Z
day: '01'
doi: 10.1038/s41557-021-00752-9
extern: '1'
external_id:
  pmid:
  - '34489564'
intvolume: '        13'
issue: '10'
keyword:
- General Chemical Engineering
- General Chemistry
language:
- iso: eng
main_file_link:
- open_access: '1'
  url: https://doi.org/10.1038/s41557-021-00752-9
month: '10'
oa: 1
oa_version: Published Version
page: 940-949
pmid: 1
publication: Nature Chemistry
publication_identifier:
  eissn:
  - 1755-4349
  issn:
  - 1755-4330
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
scopus_import: '1'
status: public
title: Electrostatic co-assembly of nanoparticles with oppositely charged small molecules
  into static and dynamic superstructures
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 13
year: '2021'
...
---
_id: '9250'
abstract:
- lang: eng
  text: Aprotic alkali metal–O2 batteries face two major obstacles to their chemistry
    occurring efficiently, the insulating nature of the formed alkali superoxides/peroxides
    and parasitic reactions that are caused by the highly reactive singlet oxygen
    (1O2). Redox mediators are recognized to be key for improving rechargeability.
    However, it is unclear how they affect 1O2 formation, which hinders strategies
    for their improvement. Here we clarify the mechanism of mediated peroxide and
    superoxide oxidation and thus explain how redox mediators either enhance or suppress
    1O2 formation. We show that charging commences with peroxide oxidation to a superoxide
    intermediate and that redox potentials above ~3.5 V versus Li/Li+ drive 1O2 evolution
    from superoxide oxidation, while disproportionation always generates some 1O2.
    We find that 1O2 suppression requires oxidation to be faster than the generation
    of 1O2 from disproportionation. Oxidation rates decrease with growing driving
    force following Marcus inverted-region behaviour, establishing a region of maximum
    rate.
acknowledged_ssus:
- _id: M-Shop
acknowledgement: S.A.F. is indebted to the European Research Council (ERC) under the
  European Union’s Horizon 2020 research and innovation programme (grant agreement
  No. 636069) as well as IST Austria. O.F thanks the French National Research Agency
  (STORE-EX Labex Project ANR-10-LABX-76-01). We thank EL-Cell GmbH (Hamburg, Germany)
  for the pressure test cell. We thank R. Saf for help with the mass spectrometry,
  J. Schlegl for manufacturing instrumentation, M. Winkler of Acib GmbH, G. Strohmeier
  and R. Fürst for HPLC measurements and S. Mondal and S. Stadlbauer for kinetic measurements.
article_processing_charge: No
article_type: original
author:
- first_name: Yann K.
  full_name: Petit, Yann K.
  last_name: Petit
- first_name: Eléonore
  full_name: Mourad, Eléonore
  last_name: Mourad
- first_name: Christian
  full_name: Prehal, Christian
  last_name: Prehal
- first_name: Christian
  full_name: Leypold, Christian
  last_name: Leypold
- first_name: Andreas
  full_name: Windischbacher, Andreas
  last_name: Windischbacher
- first_name: Daniel
  full_name: Mijailovic, Daniel
  last_name: Mijailovic
- first_name: Christian
  full_name: Slugovc, Christian
  last_name: Slugovc
- first_name: Sergey M.
  full_name: Borisov, Sergey M.
  last_name: Borisov
- first_name: Egbert
  full_name: Zojer, Egbert
  last_name: Zojer
- first_name: Sergio
  full_name: Brutti, Sergio
  last_name: Brutti
- first_name: Olivier
  full_name: Fontaine, Olivier
  last_name: Fontaine
- first_name: Stefan Alexander
  full_name: Freunberger, Stefan Alexander
  id: A8CA28E6-CE23-11E9-AD2D-EC27E6697425
  last_name: Freunberger
  orcid: 0000-0003-2902-5319
citation:
  ama: Petit YK, Mourad E, Prehal C, et al. Mechanism of mediated alkali peroxide
    oxidation and triplet versus singlet oxygen formation. <i>Nature Chemistry</i>.
    2021;13(5):465-471. doi:<a href="https://doi.org/10.1038/s41557-021-00643-z">10.1038/s41557-021-00643-z</a>
  apa: Petit, Y. K., Mourad, E., Prehal, C., Leypold, C., Windischbacher, A., Mijailovic,
    D., … Freunberger, S. A. (2021). Mechanism of mediated alkali peroxide oxidation
    and triplet versus singlet oxygen formation. <i>Nature Chemistry</i>. Springer
    Nature. <a href="https://doi.org/10.1038/s41557-021-00643-z">https://doi.org/10.1038/s41557-021-00643-z</a>
  chicago: Petit, Yann K., Eléonore Mourad, Christian Prehal, Christian Leypold, Andreas
    Windischbacher, Daniel Mijailovic, Christian Slugovc, et al. “Mechanism of Mediated
    Alkali Peroxide Oxidation and Triplet versus Singlet Oxygen Formation.” <i>Nature
    Chemistry</i>. Springer Nature, 2021. <a href="https://doi.org/10.1038/s41557-021-00643-z">https://doi.org/10.1038/s41557-021-00643-z</a>.
  ieee: Y. K. Petit <i>et al.</i>, “Mechanism of mediated alkali peroxide oxidation
    and triplet versus singlet oxygen formation,” <i>Nature Chemistry</i>, vol. 13,
    no. 5. Springer Nature, pp. 465–471, 2021.
  ista: Petit YK, Mourad E, Prehal C, Leypold C, Windischbacher A, Mijailovic D, Slugovc
    C, Borisov SM, Zojer E, Brutti S, Fontaine O, Freunberger SA. 2021. Mechanism
    of mediated alkali peroxide oxidation and triplet versus singlet oxygen formation.
    Nature Chemistry. 13(5), 465–471.
  mla: Petit, Yann K., et al. “Mechanism of Mediated Alkali Peroxide Oxidation and
    Triplet versus Singlet Oxygen Formation.” <i>Nature Chemistry</i>, vol. 13, no.
    5, Springer Nature, 2021, pp. 465–71, doi:<a href="https://doi.org/10.1038/s41557-021-00643-z">10.1038/s41557-021-00643-z</a>.
  short: Y.K. Petit, E. Mourad, C. Prehal, C. Leypold, A. Windischbacher, D. Mijailovic,
    C. Slugovc, S.M. Borisov, E. Zojer, S. Brutti, O. Fontaine, S.A. Freunberger,
    Nature Chemistry 13 (2021) 465–471.
date_created: 2021-03-16T11:12:20Z
date_published: 2021-03-15T00:00:00Z
date_updated: 2023-09-05T15:34:44Z
day: '15'
ddc:
- '540'
department:
- _id: StFr
doi: 10.1038/s41557-021-00643-z
external_id:
  isi:
  - '000629296400001'
  pmid:
  - '33723377'
file:
- access_level: open_access
  checksum: 3ee3f8dd79ed1b7bb0929fce184c8012
  content_type: application/pdf
  creator: dernst
  date_created: 2021-03-22T11:46:00Z
  date_updated: 2021-09-16T22:30:03Z
  embargo: 2021-09-15
  file_id: '9276'
  file_name: 2021_NatureChem_Petit_acceptedVersion.pdf
  file_size: 1811448
  relation: main_file
file_date_updated: 2021-09-16T22:30:03Z
has_accepted_license: '1'
intvolume: '        13'
isi: 1
issue: '5'
keyword:
- General Chemistry
- General Chemical Engineering
language:
- iso: eng
month: '03'
oa: 1
oa_version: Submitted Version
page: 465-471
pmid: 1
publication: Nature Chemistry
publication_identifier:
  eissn:
  - 1755-4349
  issn:
  - 1755-4330
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
scopus_import: '1'
status: public
title: Mechanism of mediated alkali peroxide oxidation and triplet versus singlet
  oxygen formation
type: journal_article
user_id: c635000d-4b10-11ee-a964-aac5a93f6ac1
volume: 13
year: '2021'
...
---
_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. <i>Nature Chemistry</i>. 2020;12(5):445-451.
    doi:<a href="https://doi.org/10.1038/s41557-020-0452-1">10.1038/s41557-020-0452-1</a>
  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. <i>Nature Chemistry</i>. Springer Nature.
    <a href="https://doi.org/10.1038/s41557-020-0452-1">https://doi.org/10.1038/s41557-020-0452-1</a>
  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.” <i>Nature Chemistry</i>.
    Springer Nature, 2020. <a href="https://doi.org/10.1038/s41557-020-0452-1">https://doi.org/10.1038/s41557-020-0452-1</a>.
  ieee: T. C. T. Michaels <i>et al.</i>, “Dynamics of oligomer populations formed
    during the aggregation of Alzheimer’s Aβ42 peptide,” <i>Nature Chemistry</i>,
    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.” <i>Nature Chemistry</i>, vol. 12,
    no. 5, Springer Nature, 2020, pp. 445–51, doi:<a href="https://doi.org/10.1038/s41557-020-0452-1">10.1038/s41557-020-0452-1</a>.
  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: '10360'
abstract:
- lang: eng
  text: Mapping free-energy landscapes has proved to be a powerful tool for studying
    reaction mechanisms. Many complex biomolecular assembly processes, however, have
    remained challenging to access using this approach, including the aggregation
    of peptides and proteins into amyloid fibrils implicated in a range of disorders.
    Here, we generalize the strategy used to probe free-energy landscapes in protein
    folding to determine the activation energies and entropies that characterize each
    of the molecular steps in the aggregation of the amyloid-β peptide (Aβ42), which
    is associated with Alzheimer’s disease. Our results reveal that interactions between
    monomeric Aβ42 and amyloid fibrils during fibril-dependent secondary nucleation
    fundamentally reverse the thermodynamic signature of this process relative to
    primary nucleation, even though both processes generate aggregates from soluble
    peptides. By mapping the energetic and entropic contributions along the reaction
    trajectories, we show that the catalytic efficiency of Aβ42 fibril surfaces results
    from the enthalpic stabilization of adsorbing peptides in conformations amenable
    to nucleation, resulting in a dramatic lowering of the activation energy for nucleation.
acknowledgement: We thank B. Jönsson and I. André for helpful discussions. We acknowledge
  financial support from the Schiff Foundation (S.I.A.C.), St John’s College, Cambridge
  (S.I.A.C.), the Royal Physiographic Society (R.C.), the Research School FLÄK of
  Lund University (S.L., R.C.), the Swedish Research Council (S.L.) and its Linneaus
  Centre Organizing Molecular Matter (S.L.), the Crafoord Foundation (S.L.), Alzheimerfonden
  (S.L.), the European Research Council (S.L.), NanoLund (S.L.), Knut and Alice Wallenberg
  Foundation (S.L.), Peterhouse, Cambridge (T.C.T.M.), the Swiss National Science
  Foundation (T.C.T.M.), Magdalene College, Cambridge (A.K.B.), the Leverhulme Trust
  (A.K.B.), the Royal Society (A.Š.), the Academy of Medical Sciences (A.Š.), the
  Wellcome Trust (C.M.D., T.P.J.K., A.Š.), and the Centre for Misfolding Diseases
  (C.M.D., T.P.J.K, M.V.). A.K.B. thanks the Alzheimer Forschung Initiative (AFI).
article_processing_charge: No
article_type: original
author:
- first_name: Samuel I. A.
  full_name: Cohen, Samuel I. A.
  last_name: Cohen
- first_name: Risto
  full_name: Cukalevski, Risto
  last_name: Cukalevski
- 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: Mattias
  full_name: Törnquist, Mattias
  last_name: Törnquist
- first_name: Michele
  full_name: Vendruscolo, Michele
  last_name: Vendruscolo
- first_name: Christopher M.
  full_name: Dobson, Christopher M.
  last_name: Dobson
- first_name: Alexander K.
  full_name: Buell, Alexander K.
  last_name: Buell
- first_name: Tuomas P. J.
  full_name: Knowles, Tuomas P. J.
  last_name: Knowles
- first_name: Sara
  full_name: Linse, Sara
  last_name: Linse
citation:
  ama: Cohen SIA, Cukalevski R, Michaels TCT, et al. Distinct thermodynamic signatures
    of oligomer generation in the aggregation of the amyloid-β peptide. <i>Nature
    Chemistry</i>. 2018;10(5):523-531. doi:<a href="https://doi.org/10.1038/s41557-018-0023-x">10.1038/s41557-018-0023-x</a>
  apa: Cohen, S. I. A., Cukalevski, R., Michaels, T. C. T., Šarić, A., Törnquist,
    M., Vendruscolo, M., … Linse, S. (2018). Distinct thermodynamic signatures of
    oligomer generation in the aggregation of the amyloid-β peptide. <i>Nature Chemistry</i>.
    Springer Nature. <a href="https://doi.org/10.1038/s41557-018-0023-x">https://doi.org/10.1038/s41557-018-0023-x</a>
  chicago: Cohen, Samuel I. A., Risto Cukalevski, Thomas C. T. Michaels, Anđela Šarić,
    Mattias Törnquist, Michele Vendruscolo, Christopher M. Dobson, Alexander K. Buell,
    Tuomas P. J. Knowles, and Sara Linse. “Distinct Thermodynamic Signatures of Oligomer
    Generation in the Aggregation of the Amyloid-β Peptide.” <i>Nature Chemistry</i>.
    Springer Nature, 2018. <a href="https://doi.org/10.1038/s41557-018-0023-x">https://doi.org/10.1038/s41557-018-0023-x</a>.
  ieee: S. I. A. Cohen <i>et al.</i>, “Distinct thermodynamic signatures of oligomer
    generation in the aggregation of the amyloid-β peptide,” <i>Nature Chemistry</i>,
    vol. 10, no. 5. Springer Nature, pp. 523–531, 2018.
  ista: Cohen SIA, Cukalevski R, Michaels TCT, Šarić A, Törnquist M, Vendruscolo M,
    Dobson CM, Buell AK, Knowles TPJ, Linse S. 2018. Distinct thermodynamic signatures
    of oligomer generation in the aggregation of the amyloid-β peptide. Nature Chemistry.
    10(5), 523–531.
  mla: Cohen, Samuel I. A., et al. “Distinct Thermodynamic Signatures of Oligomer
    Generation in the Aggregation of the Amyloid-β Peptide.” <i>Nature Chemistry</i>,
    vol. 10, no. 5, Springer Nature, 2018, pp. 523–31, doi:<a href="https://doi.org/10.1038/s41557-018-0023-x">10.1038/s41557-018-0023-x</a>.
  short: S.I.A. Cohen, R. Cukalevski, T.C.T. Michaels, A. Šarić, M. Törnquist, M.
    Vendruscolo, C.M. Dobson, A.K. Buell, T.P.J. Knowles, S. Linse, Nature Chemistry
    10 (2018) 523–531.
date_created: 2021-11-26T12:41:38Z
date_published: 2018-03-26T00:00:00Z
date_updated: 2021-11-26T15:14:00Z
day: '26'
doi: 10.1038/s41557-018-0023-x
extern: '1'
external_id:
  pmid:
  - '29581486'
intvolume: '        10'
issue: '5'
keyword:
- general chemical engineering
- general chemistry
language:
- iso: eng
month: '03'
oa_version: None
page: 523-531
pmid: 1
publication: Nature Chemistry
publication_identifier:
  eissn:
  - 1755-4349
  issn:
  - 1755-4330
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
scopus_import: '1'
status: public
title: Distinct thermodynamic signatures of oligomer generation in the aggregation
  of the amyloid-β peptide
type: journal_article
user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9
volume: 10
year: '2018'
...
---
_id: '13394'
abstract:
- lang: eng
  text: The ability to guide the assembly of nanosized objects reversibly with external
    stimuli, in particular light, is of fundamental importance, and it contributes
    to the development of applications as diverse as nanofabrication and controlled
    drug delivery. However, all the systems described to date are based on nanoparticles
    (NPs) that are inherently photoresponsive, which makes their preparation cumbersome
    and can markedly hamper their performance. Here we describe a conceptually new
    methodology to assemble NPs reversibly using light that does not require the particles
    to be functionalized with light-responsive ligands. Our strategy is based on the
    use of a photoswitchable medium that responds to light in such a way that it modulates
    the interparticle interactions. NP assembly proceeds quantitatively and without
    apparent fatigue, both in solution and in gels. Exposing the gels to light in
    a spatially controlled manner allowed us to draw images that spontaneously disappeared
    after a specific period of time.
article_processing_charge: No
article_type: original
author:
- first_name: Pintu K.
  full_name: Kundu, Pintu K.
  last_name: Kundu
- first_name: Dipak
  full_name: Samanta, Dipak
  last_name: Samanta
- first_name: Ron
  full_name: Leizrowice, Ron
  last_name: Leizrowice
- first_name: Baruch
  full_name: Margulis, Baruch
  last_name: Margulis
- first_name: Hui
  full_name: Zhao, Hui
  last_name: Zhao
- first_name: Martin
  full_name: Börner, Martin
  last_name: Börner
- first_name: T.
  full_name: Udayabhaskararao, T.
  last_name: Udayabhaskararao
- first_name: Debasish
  full_name: Manna, Debasish
  last_name: Manna
- first_name: Rafal
  full_name: Klajn, Rafal
  id: 8e84690e-1e48-11ed-a02b-a1e6fb8bb53b
  last_name: Klajn
citation:
  ama: Kundu PK, Samanta D, Leizrowice R, et al. Light-controlled self-assembly of
    non-photoresponsive nanoparticles. <i>Nature Chemistry</i>. 2015;7:646-652. doi:<a
    href="https://doi.org/10.1038/nchem.2303">10.1038/nchem.2303</a>
  apa: Kundu, P. K., Samanta, D., Leizrowice, R., Margulis, B., Zhao, H., Börner,
    M., … Klajn, R. (2015). Light-controlled self-assembly of non-photoresponsive
    nanoparticles. <i>Nature Chemistry</i>. Springer Nature. <a href="https://doi.org/10.1038/nchem.2303">https://doi.org/10.1038/nchem.2303</a>
  chicago: Kundu, Pintu K., Dipak Samanta, Ron Leizrowice, Baruch Margulis, Hui Zhao,
    Martin Börner, T. Udayabhaskararao, Debasish Manna, and Rafal Klajn. “Light-Controlled
    Self-Assembly of Non-Photoresponsive Nanoparticles.” <i>Nature Chemistry</i>.
    Springer Nature, 2015. <a href="https://doi.org/10.1038/nchem.2303">https://doi.org/10.1038/nchem.2303</a>.
  ieee: P. K. Kundu <i>et al.</i>, “Light-controlled self-assembly of non-photoresponsive
    nanoparticles,” <i>Nature Chemistry</i>, vol. 7. Springer Nature, pp. 646–652,
    2015.
  ista: Kundu PK, Samanta D, Leizrowice R, Margulis B, Zhao H, Börner M, Udayabhaskararao
    T, Manna D, Klajn R. 2015. Light-controlled self-assembly of non-photoresponsive
    nanoparticles. Nature Chemistry. 7, 646–652.
  mla: Kundu, Pintu K., et al. “Light-Controlled Self-Assembly of Non-Photoresponsive
    Nanoparticles.” <i>Nature Chemistry</i>, vol. 7, Springer Nature, 2015, pp. 646–52,
    doi:<a href="https://doi.org/10.1038/nchem.2303">10.1038/nchem.2303</a>.
  short: P.K. Kundu, D. Samanta, R. Leizrowice, B. Margulis, H. Zhao, M. Börner, T.
    Udayabhaskararao, D. Manna, R. Klajn, Nature Chemistry 7 (2015) 646–652.
date_created: 2023-08-01T09:44:33Z
date_published: 2015-07-20T00:00:00Z
date_updated: 2023-08-07T13:00:15Z
day: '20'
doi: 10.1038/nchem.2303
extern: '1'
external_id:
  pmid:
  - '26201741'
intvolume: '         7'
keyword:
- General Chemical Engineering
- General Chemistry
language:
- iso: eng
month: '07'
oa_version: None
page: 646-652
pmid: 1
publication: Nature Chemistry
publication_identifier:
  eissn:
  - 1755-4349
  issn:
  - 1755-4330
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
scopus_import: '1'
status: public
title: Light-controlled self-assembly of non-photoresponsive nanoparticles
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 7
year: '2015'
...
---
_id: '13415'
abstract:
- lang: eng
  text: Systems in which nanoscale components of different types can be captured and/or
    released from organic scaffolds provide a fertile basis for the construction of
    dynamic, exchangeable functional materials. In such heterogeneous systems, the
    components interact with one another by means of programmable, noncovalent bonding
    interactions. Herein, we describe polymers that capture and release functionalized
    nanoparticles selectively during redox-controlled aggregation and disaggregation,
    respectively. The interactions between the polymer and the NPs are mediated by
    the reversible formation of polypseudorotaxanes, and give rise to architectures
    ranging from short chains composed of few nanoparticles to extended networks of
    nanoparticles crosslinked by the polymer. In the latter case, the polymer/nanoparticle
    aggregates precipitate from solution such that the polymer acts as a selective
    ‘sponge’ for the capture/release of the nanoparticles of different types.
article_processing_charge: No
article_type: original
author:
- first_name: Rafal
  full_name: Klajn, Rafal
  id: 8e84690e-1e48-11ed-a02b-a1e6fb8bb53b
  last_name: Klajn
- first_name: Mark A.
  full_name: Olson, Mark A.
  last_name: Olson
- first_name: Paul J.
  full_name: Wesson, Paul J.
  last_name: Wesson
- first_name: Lei
  full_name: Fang, Lei
  last_name: Fang
- first_name: Ali
  full_name: Coskun, Ali
  last_name: Coskun
- first_name: Ali
  full_name: Trabolsi, Ali
  last_name: Trabolsi
- first_name: Siowling
  full_name: Soh, Siowling
  last_name: Soh
- first_name: J. Fraser
  full_name: Stoddart, J. Fraser
  last_name: Stoddart
- first_name: Bartosz A.
  full_name: Grzybowski, Bartosz A.
  last_name: Grzybowski
citation:
  ama: Klajn R, Olson MA, Wesson PJ, et al. Dynamic hook-and-eye nanoparticle sponges.
    <i>Nature Chemistry</i>. 2009;1:733-738. doi:<a href="https://doi.org/10.1038/nchem.432">10.1038/nchem.432</a>
  apa: Klajn, R., Olson, M. A., Wesson, P. J., Fang, L., Coskun, A., Trabolsi, A.,
    … Grzybowski, B. A. (2009). Dynamic hook-and-eye nanoparticle sponges. <i>Nature
    Chemistry</i>. Springer Nature. <a href="https://doi.org/10.1038/nchem.432">https://doi.org/10.1038/nchem.432</a>
  chicago: Klajn, Rafal, Mark A. Olson, Paul J. Wesson, Lei Fang, Ali Coskun, Ali
    Trabolsi, Siowling Soh, J. Fraser Stoddart, and Bartosz A. Grzybowski. “Dynamic
    Hook-and-Eye Nanoparticle Sponges.” <i>Nature Chemistry</i>. Springer Nature,
    2009. <a href="https://doi.org/10.1038/nchem.432">https://doi.org/10.1038/nchem.432</a>.
  ieee: R. Klajn <i>et al.</i>, “Dynamic hook-and-eye nanoparticle sponges,” <i>Nature
    Chemistry</i>, vol. 1. Springer Nature, pp. 733–738, 2009.
  ista: Klajn R, Olson MA, Wesson PJ, Fang L, Coskun A, Trabolsi A, Soh S, Stoddart
    JF, Grzybowski BA. 2009. Dynamic hook-and-eye nanoparticle sponges. Nature Chemistry.
    1, 733–738.
  mla: Klajn, Rafal, et al. “Dynamic Hook-and-Eye Nanoparticle Sponges.” <i>Nature
    Chemistry</i>, vol. 1, Springer Nature, 2009, pp. 733–38, doi:<a href="https://doi.org/10.1038/nchem.432">10.1038/nchem.432</a>.
  short: R. Klajn, M.A. Olson, P.J. Wesson, L. Fang, A. Coskun, A. Trabolsi, S. Soh,
    J.F. Stoddart, B.A. Grzybowski, Nature Chemistry 1 (2009) 733–738.
date_created: 2023-08-01T09:50:23Z
date_published: 2009-12-01T00:00:00Z
date_updated: 2023-08-08T08:55:36Z
day: '01'
doi: 10.1038/nchem.432
extern: '1'
external_id:
  pmid:
  - '21124361'
intvolume: '         1'
keyword:
- General Chemical Engineering
- General Chemistry
language:
- iso: eng
month: '12'
oa_version: None
page: 733-738
pmid: 1
publication: Nature Chemistry
publication_identifier:
  eissn:
  - 1755-4349
  issn:
  - 1755-4330
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
scopus_import: '1'
status: public
title: Dynamic hook-and-eye nanoparticle sponges
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 1
year: '2009'
...
