Kinetic control of parallel versus antiparallel amyloid aggregation via shape of the growing aggregate
Abstract: By combining atomistic and higher-level modelling with solution X-ray diffraction we analyse self-assembly pathways for the IFQINS hexapeptide, a bio-relevant amyloid former derived from human lysozyme. We verify that (at least) two metastable polymorphic structures exist for this system which are substantially different at the atomistic scale, and compare the conditions under which they are kinetically accessible. We further examine the higher-level polymorphism for these systems at the nanometre to micrometre scales, which is manifested in kinetic differences and in shape differences between structures instead of or as well as differences in the small-scale contact topology. Any future design of structure based inhibitors of the IFQINS steric zipper, or of close homologues such as TFQINS which are likely to have similar structures, should take account of this polymorphic assembly
- Location
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Deutsche Nationalbibliothek Frankfurt am Main
- Extent
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Online-Ressource
- Language
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Englisch
- Notes
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Scientific reports. - 9, 1 (2019) , ISSN: 2045-2322
- Event
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Veröffentlichung
- (where)
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Freiburg
- (who)
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Universität
- (when)
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2020
- Creator
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Zanjani, Ali Asghar Hakami
Reynolds, Nicholas P.
Zhang, Afang
Schilling, Tanja
Mezzenga, Raffaele
Berryman, Joshua T.
- Contributor
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Arbeitsgruppe Statistische Physik Weicher Materie und Komplexer Systeme
- DOI
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10.1038/s41598-019-52238-x
- URN
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urn:nbn:de:bsz:25-freidok-1709506
- Rights
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Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
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14.08.2025, 10:46 AM CEST
Data provider
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Associated
- Zanjani, Ali Asghar Hakami
- Reynolds, Nicholas P.
- Zhang, Afang
- Schilling, Tanja
- Mezzenga, Raffaele
- Berryman, Joshua T.
- Arbeitsgruppe Statistische Physik Weicher Materie und Komplexer Systeme
- Universität
Time of origin
- 2020