Dimers of D76N-β₂-microglobulin display potent antiamyloid aggregation activity.

ABSTRACT: Self-association of WT β_2-microglobulin (WT-β₂m) into amyloid fibrils is associated with the disorder dialysis related amyloidosis. In the familial variant D76N-β₂m, the single amino acid substitution enhances the aggregation propensity of the protein dramatically and gives rise to a disorder that is independent of renal dysfunction. Numerous biophysical and structural studies on WT- and D76N-β₂m have been performed in order to better understand the structure and dynamics of the native proteins and their different potentials to aggregate into amyloid. However, the structural properties of transient D76N-β₂m oligomers and their role(s) in assembly remained uncharted. Here, we have utilized NMR methods, combined with photo-induced crossl

SUBMITTER: Maya-Martinez R 

PROVIDER: S-EPMC9712992 | biostudies-literature | 2022 Dec

REPOSITORIES: biostudies-literature