Collagen I Weakly Interacts with the β-Sheets of β₂-Microglobulin and Enhances Conformational Exchange To Induce Amyloid Formation.

ABSTRACT: Amyloidogenesis is significant in both protein function and pathology. Amyloid formation of folded, globular proteins is commonly initiated by partial or complete unfolding. However, how this unfolding event is triggered for proteins that are otherwise stable in their native environments is not well understood. The accumulation of the immunoglobulin protein β₂-microglobulin (β₂m) into amyloid plaques in the joints of long-term hemodialysis patients is the hallmark of dialysis-related amyloidosis (DRA). While β₂m does not form amyloid unassisted near neutral pH in vitro, the localization of β₂m deposits to joint spaces suggests a role for the local extracellular matrix (ECM) proteins, specifically collagens, in promoting amyloid formation.

SUBMITTER: Hoop CL 

PROVIDER: S-EPMC7135851 | biostudies-literature | 2020 Jan

REPOSITORIES: biostudies-literature