Ontology highlight
ABSTRACT:
SUBMITTER: Bunce SJ
PROVIDER: S-EPMC6588359 | biostudies-literature | 2019 Jun
REPOSITORIES: biostudies-literature
Bunce Samuel J SJ Wang Yiming Y Stewart Katie L KL Ashcroft Alison E AE Radford Sheena E SE Hall Carol K CK Wilson Andrew J AJ
Science advances 20190621 6
Understanding the structural mechanism by which proteins and peptides aggregate is crucial, given the role of fibrillar aggregates in debilitating amyloid diseases and bioinspired materials. Yet, this is a major challenge as the assembly involves multiple heterogeneous and transient intermediates. Here, we analyze the co-aggregation of Aβ<sub>40</sub> and Aβ<sub>16-22</sub>, two widely studied peptide fragments of Aβ<sub>42</sub> implicated in Alzheimer's disease. We demonstrate that Aβ<sub>16-2 ...[more]