A synchrotron-based hydroxyl radical footprinting analysis of amyloid fibrils and prefibrillar intermediates with residue-specific resolution.

ABSTRACT: Structural models of the fibrils formed by the 40-residue amyloid-β (Aβ40) peptide in Alzheimer's disease typically consist of linear polypeptide segments, oriented approximately perpendicular to the long axis of the fibril, and joined together as parallel in-register β-sheets to form filaments. However, various models differ in the number of filaments that run the length of a fibril, and in the topological arrangement of these filaments. In addition to questions about the structure of Aβ40 monomers in fibrils, there are important unanswered questions about their structure in prefibrillar intermediates, which are of interest because they may represent the most neurotoxic form of Aβ40. To assess different models of fibril structure and to gain insight into the structure of prefibrillar inte

SUBMITTER: Klinger AL 

PROVIDER: S-EPMC4270378 | biostudies-literature | 2014 Dec

REPOSITORIES: biostudies-literature