Site specific NMR characterization of abeta-40 oligomers cross seeded by abeta-42 oligomers† † Electronic supplementary information (ESI) available. See https://doi.org/10.1039/d2sc01555b

ABSTRACT: Extracellular accumulation of β amyloid peptides of 40 (Aβ40) and 42 residues (Aβ42) has been considered as one of the hallmarks in the pathology of Alzheimer's disease. In this work, we are able to prepare oligomeric aggregates of Aβ with uniform size and monomorphic structure. Our experimental design is to incubate Aβ peptides in reverse micelles (RMs) so that the peptides could aggregate only through a single nucleation process and the size of the oligomers is confined by the physical dimension of the reverse micelles. The hence obtained Aβ oligomers (AβOs) are 23 nm in diameter and they belong to the category of high molecular-weight (MW) oligomers. The solid-state NMR data revealed that Aβ40Os adopt the structural motif of β-loop-β but the chemical shifts manifested that they may be s

SUBMITTER: Chang H 

PROVIDER: S-EPMC9337746 | biostudies-literature | 2022 Jun

REPOSITORIES: biostudies-literature