Nanoscale Structural Analysis of a Lipid-Driven Aggregation of Insulin.

ABSTRACT: Abrupt aggregation of misfolded proteins is a hallmark of a large number of severe pathologies, including diabetes types 1 and 2, Alzheimer, and Parkinson diseases. A growing body of evidence suggests that lipids can uniquely change rates of amyloid-associated proteins as well as modify the structure of formed oligomers and fibrils. In this study, we utilize atomic force microscopy infrared (AFM-IR) spectroscopy, also known as nano-IR spectroscopy, to examine the structure of individual insulin oligomers, protofilaments, and fibrils grown in the presence of phospholipids. Our findings show that AFM-IR spectra of insulin oligomers have strong signals of C-H and PO₂^- vibrations, which points on the presence of lipids in the oligomer structure. Furthermore, substantial s

SUBMITTER: Rizevsky S 

PROVIDER: S-EPMC9169669 | biostudies-literature | 2022 Mar

REPOSITORIES: biostudies-literature