Intermediate antiparallel beta structure in amyloid plaques revealed by infrared spectroscopic imaging.

ABSTRACT: Aggregation of amyloid beta (Aβ) peptides into extracellular plaques is a hallmark of the molecular pathology of Alzheimer's disease (AD). Amyloid aggregates have been extensively studied in-vitro, and it is well known that mature amyloid fibrils contain an ordered parallel β structure. The structural evolution from unaggregated peptide to fibrils can be mediated through intermediate structures that deviate significantly from mature fibrils, such as antiparallel β-sheets. However, it is currently unknown if these intermediate structures exist in plaques, which limits the translation of findings from in-vitro structural characterizations of amyloid aggregates to AD. This arises from the inability to extend common structural biology techniques to ex-vivo tissue measurements. Here we report t

SUBMITTER: Holcombe B 

PROVIDER: S-EPMC10153194 | biostudies-literature | 2023 Apr

REPOSITORIES: biostudies-literature