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
Deutsche Nationalbibliothek Frankfurt am Main
Extent
Online-Ressource
Language
Englisch
Notes
Scientific reports. - 9, 1 (2019) , ISSN: 2045-2322

Event
Veröffentlichung
(where)
Freiburg
(who)
Universität
(when)
2020
Creator
Zanjani, Ali Asghar Hakami
Reynolds, Nicholas P.
Zhang, Afang
Schilling, Tanja
Mezzenga, Raffaele
Berryman, Joshua T.
Contributor
Arbeitsgruppe Statistische Physik Weicher Materie und Komplexer Systeme

DOI
10.1038/s41598-019-52238-x
URN
urn:nbn:de:bsz:25-freidok-1709506
Rights
Der Zugriff auf das Objekt ist unbeschränkt möglich.
Last update
14.08.2025, 10:46 AM CEST

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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

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