[{"publication_status":"published","page":"940-949","oa_version":"Published Version","day":"01","abstract":[{"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.","lang":"eng"}],"status":"public","date_updated":"2023-08-02T10:55:29Z","publication":"Nature Chemistry","external_id":{"pmid":["34489564"]},"title":"Electrostatic co-assembly of nanoparticles with oppositely charged small molecules into static and dynamic superstructures","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1038/s41557-021-00752-9"}],"issue":"10","scopus_import":"1","citation":{"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.","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>","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.","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.","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>.","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>"},"date_published":"2021-10-01T00:00:00Z","author":[{"last_name":"Bian","full_name":"Bian, Tong","first_name":"Tong"},{"full_name":"Gardin, Andrea","first_name":"Andrea","last_name":"Gardin"},{"full_name":"Gemen, Julius","first_name":"Julius","last_name":"Gemen"},{"last_name":"Houben","full_name":"Houben, Lothar","first_name":"Lothar"},{"full_name":"Perego, Claudio","first_name":"Claudio","last_name":"Perego"},{"last_name":"Lee","full_name":"Lee, Byeongdu","first_name":"Byeongdu"},{"first_name":"Nadav","full_name":"Elad, Nadav","last_name":"Elad"},{"first_name":"Zonglin","full_name":"Chu, Zonglin","last_name":"Chu"},{"last_name":"Pavan","first_name":"Giovanni M.","full_name":"Pavan, Giovanni M."},{"id":"8e84690e-1e48-11ed-a02b-a1e6fb8bb53b","last_name":"Klajn","first_name":"Rafal","full_name":"Klajn, Rafal"}],"oa":1,"_id":"13357","type":"journal_article","language":[{"iso":"eng"}],"doi":"10.1038/s41557-021-00752-9","publisher":"Springer Nature","year":"2021","article_type":"original","volume":13,"month":"10","quality_controlled":"1","publication_identifier":{"eissn":["1755-4349"],"issn":["1755-4330"]},"article_processing_charge":"No","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","extern":"1","keyword":["General Chemical Engineering","General Chemistry"],"intvolume":"        13","date_created":"2023-08-01T09:34:54Z","pmid":1},{"quality_controlled":"1","publication_identifier":{"eissn":["1755-4349"],"issn":["1755-4330"]},"month":"03","volume":13,"article_type":"original","isi":1,"pmid":1,"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.","department":[{"_id":"StFr"}],"date_created":"2021-03-16T11:12:20Z","keyword":["General Chemistry","General Chemical Engineering"],"intvolume":"        13","user_id":"c635000d-4b10-11ee-a964-aac5a93f6ac1","article_processing_charge":"No","ddc":["540"],"file_date_updated":"2021-09-16T22:30:03Z","oa":1,"_id":"9250","author":[{"first_name":"Yann K.","full_name":"Petit, Yann K.","last_name":"Petit"},{"last_name":"Mourad","first_name":"Eléonore","full_name":"Mourad, Eléonore"},{"full_name":"Prehal, Christian","first_name":"Christian","last_name":"Prehal"},{"last_name":"Leypold","first_name":"Christian","full_name":"Leypold, Christian"},{"last_name":"Windischbacher","full_name":"Windischbacher, Andreas","first_name":"Andreas"},{"full_name":"Mijailovic, Daniel","first_name":"Daniel","last_name":"Mijailovic"},{"full_name":"Slugovc, Christian","first_name":"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"},{"last_name":"Brutti","full_name":"Brutti, Sergio","first_name":"Sergio"},{"full_name":"Fontaine, Olivier","first_name":"Olivier","last_name":"Fontaine"},{"orcid":"0000-0003-2902-5319","id":"A8CA28E6-CE23-11E9-AD2D-EC27E6697425","last_name":"Freunberger","first_name":"Stefan Alexander","full_name":"Freunberger, Stefan Alexander"}],"date_published":"2021-03-15T00:00:00Z","publisher":"Springer Nature","year":"2021","language":[{"iso":"eng"}],"doi":"10.1038/s41557-021-00643-z","type":"journal_article","external_id":{"isi":["000629296400001"],"pmid":["33723377"]},"title":"Mechanism of mediated alkali peroxide oxidation and triplet versus singlet oxygen formation","file":[{"embargo":"2021-09-15","creator":"dernst","access_level":"open_access","relation":"main_file","content_type":"application/pdf","file_name":"2021_NatureChem_Petit_acceptedVersion.pdf","file_size":1811448,"date_created":"2021-03-22T11:46:00Z","file_id":"9276","checksum":"3ee3f8dd79ed1b7bb0929fce184c8012","date_updated":"2021-09-16T22:30:03Z"}],"publication":"Nature Chemistry","citation":{"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.","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>.","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>","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.","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.","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>"},"has_accepted_license":"1","issue":"5","scopus_import":"1","abstract":[{"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.","lang":"eng"}],"page":"465-471","oa_version":"Submitted Version","publication_status":"published","day":"15","date_updated":"2023-09-05T15:34:44Z","acknowledged_ssus":[{"_id":"M-Shop"}],"status":"public"},{"abstract":[{"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.","lang":"eng"}],"oa_version":"None","publication_status":"published","page":"445-451","day":"13","status":"public","date_updated":"2021-11-26T11:21:08Z","related_material":{"link":[{"relation":"erratum","url":"https://doi.org/10.1038/s41557-020-0468-6"}]},"external_id":{"pmid":["32303714"]},"title":"Dynamics of oligomer populations formed during the aggregation of Alzheimer’s Aβ42 peptide","publication":"Nature Chemistry","main_file_link":[{"open_access":"1","url":"https://www.biorxiv.org/content/10.1101/2020.01.08.897488"}],"issue":"5","scopus_import":"1","citation":{"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.","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.","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>.","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>","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>"},"date_published":"2020-04-13T00:00:00Z","oa":1,"_id":"10351","author":[{"first_name":"Thomas C. T.","full_name":"Michaels, Thomas C. T.","last_name":"Michaels"},{"orcid":"0000-0002-7854-2139","last_name":"Šarić","id":"bf63d406-f056-11eb-b41d-f263a6566d8b","full_name":"Šarić, Anđela","first_name":"Anđela"},{"full_name":"Curk, Samo","first_name":"Samo","last_name":"Curk"},{"last_name":"Bernfur","first_name":"Katja","full_name":"Bernfur, Katja"},{"last_name":"Arosio","first_name":"Paolo","full_name":"Arosio, Paolo"},{"full_name":"Meisl, Georg","first_name":"Georg","last_name":"Meisl"},{"last_name":"Dear","first_name":"Alexander J.","full_name":"Dear, Alexander J."},{"first_name":"Samuel I. A.","full_name":"Cohen, Samuel I. A.","last_name":"Cohen"},{"last_name":"Dobson","full_name":"Dobson, Christopher M.","first_name":"Christopher M."},{"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"}],"type":"journal_article","publisher":"Springer Nature","year":"2020","language":[{"iso":"eng"}],"doi":"10.1038/s41557-020-0452-1","volume":12,"article_type":"original","quality_controlled":"1","publication_identifier":{"issn":["1755-4330"],"eissn":["1755-4349"]},"month":"04","keyword":["general chemical engineering","general chemistry"],"intvolume":"        12","article_processing_charge":"No","user_id":"8b945eb4-e2f2-11eb-945a-df72226e66a9","extern":"1","pmid":1,"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).","date_created":"2021-11-26T09:15:13Z"},{"month":"03","quality_controlled":"1","publication_identifier":{"issn":["1755-4330"],"eissn":["1755-4349"]},"volume":10,"article_type":"original","date_created":"2021-11-26T12:41:38Z","pmid":1,"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).","extern":"1","article_processing_charge":"No","user_id":"8b945eb4-e2f2-11eb-945a-df72226e66a9","keyword":["general chemical engineering","general chemistry"],"intvolume":"        10","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"},{"full_name":"Michaels, Thomas C. T.","first_name":"Thomas C. T.","last_name":"Michaels"},{"id":"bf63d406-f056-11eb-b41d-f263a6566d8b","last_name":"Šarić","orcid":"0000-0002-7854-2139","full_name":"Šarić, Anđela","first_name":"Anđela"},{"first_name":"Mattias","full_name":"Törnquist, Mattias","last_name":"Törnquist"},{"last_name":"Vendruscolo","first_name":"Michele","full_name":"Vendruscolo, Michele"},{"last_name":"Dobson","first_name":"Christopher M.","full_name":"Dobson, Christopher M."},{"first_name":"Alexander K.","full_name":"Buell, Alexander K.","last_name":"Buell"},{"last_name":"Knowles","full_name":"Knowles, Tuomas P. J.","first_name":"Tuomas P. J."},{"last_name":"Linse","first_name":"Sara","full_name":"Linse, Sara"}],"_id":"10360","date_published":"2018-03-26T00:00:00Z","language":[{"iso":"eng"}],"doi":"10.1038/s41557-018-0023-x","publisher":"Springer Nature","year":"2018","type":"journal_article","publication":"Nature Chemistry","external_id":{"pmid":["29581486"]},"title":"Distinct thermodynamic signatures of oligomer generation in the aggregation of the amyloid-β peptide","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>","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.","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>","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.","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>.","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.","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>."},"issue":"5","scopus_import":"1","oa_version":"None","publication_status":"published","page":"523-531","day":"26","abstract":[{"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.","lang":"eng"}],"date_updated":"2021-11-26T15:14:00Z","status":"public"},{"author":[{"last_name":"Kundu","full_name":"Kundu, Pintu K.","first_name":"Pintu K."},{"full_name":"Samanta, Dipak","first_name":"Dipak","last_name":"Samanta"},{"last_name":"Leizrowice","first_name":"Ron","full_name":"Leizrowice, Ron"},{"last_name":"Margulis","full_name":"Margulis, Baruch","first_name":"Baruch"},{"last_name":"Zhao","first_name":"Hui","full_name":"Zhao, Hui"},{"full_name":"Börner, Martin","first_name":"Martin","last_name":"Börner"},{"first_name":"T.","full_name":"Udayabhaskararao, T.","last_name":"Udayabhaskararao"},{"last_name":"Manna","full_name":"Manna, Debasish","first_name":"Debasish"},{"full_name":"Klajn, Rafal","first_name":"Rafal","last_name":"Klajn","id":"8e84690e-1e48-11ed-a02b-a1e6fb8bb53b"}],"_id":"13394","date_published":"2015-07-20T00:00:00Z","language":[{"iso":"eng"}],"doi":"10.1038/nchem.2303","publisher":"Springer Nature","year":"2015","type":"journal_article","month":"07","quality_controlled":"1","publication_identifier":{"eissn":["1755-4349"],"issn":["1755-4330"]},"volume":7,"article_type":"original","date_created":"2023-08-01T09:44:33Z","pmid":1,"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","article_processing_charge":"No","extern":"1","keyword":["General Chemical Engineering","General Chemistry"],"intvolume":"         7","oa_version":"None","publication_status":"published","page":"646-652","day":"20","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."}],"date_updated":"2023-08-07T13:00:15Z","status":"public","publication":"Nature Chemistry","external_id":{"pmid":["26201741"]},"title":"Light-controlled self-assembly of non-photoresponsive nanoparticles","citation":{"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>.","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>","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.","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>","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."},"scopus_import":"1"},{"date_published":"2009-12-01T00:00:00Z","_id":"13415","author":[{"first_name":"Rafal","full_name":"Klajn, Rafal","last_name":"Klajn","id":"8e84690e-1e48-11ed-a02b-a1e6fb8bb53b"},{"first_name":"Mark A.","full_name":"Olson, Mark A.","last_name":"Olson"},{"last_name":"Wesson","first_name":"Paul J.","full_name":"Wesson, Paul J."},{"last_name":"Fang","first_name":"Lei","full_name":"Fang, Lei"},{"first_name":"Ali","full_name":"Coskun, Ali","last_name":"Coskun"},{"first_name":"Ali","full_name":"Trabolsi, Ali","last_name":"Trabolsi"},{"last_name":"Soh","first_name":"Siowling","full_name":"Soh, Siowling"},{"last_name":"Stoddart","full_name":"Stoddart, J. Fraser","first_name":"J. Fraser"},{"first_name":"Bartosz A.","full_name":"Grzybowski, Bartosz A.","last_name":"Grzybowski"}],"type":"journal_article","year":"2009","publisher":"Springer Nature","doi":"10.1038/nchem.432","language":[{"iso":"eng"}],"article_type":"original","volume":1,"publication_identifier":{"eissn":["1755-4349"],"issn":["1755-4330"]},"quality_controlled":"1","month":"12","intvolume":"         1","keyword":["General Chemical Engineering","General Chemistry"],"extern":"1","article_processing_charge":"No","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","pmid":1,"date_created":"2023-08-01T09:50:23Z","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."}],"day":"01","publication_status":"published","page":"733-738","oa_version":"None","status":"public","date_updated":"2023-08-08T08:55:36Z","title":"Dynamic hook-and-eye nanoparticle sponges","external_id":{"pmid":["21124361"]},"publication":"Nature Chemistry","scopus_import":"1","citation":{"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.","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>.","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>","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.","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>.","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."}}]