Amyloid-beta peptide (25-35) triggers a reorganization of lipid membranes driven by temperature changes.

ABSTRACT: The amyloid-beta peptide (Aβ) is considered a key factor in Alzheimer's disease (AD) ever since the discovery of the disease. The understanding of its damaging influence has however shifted recently from large fibrils observed in the inter-cellular environment to the small oligomers interacting with a cell membrane. We studied the effect of temperature on the latter interactions by evaluating the structural characteristics of zwitterionic phosphatidylcholine (PC) membranes with incorporated Aβ_25-35 peptide. By means of small angle neutron scattering (SANS), we have observed for the first time a spontaneous reformation of extruded unilamellar vesicles (EULVs) to discoidal bicelle-like structures (BLSs) and small unilamellar vesicles (SULVs). These changes in the membrane self-org

SUBMITTER: Ivankov O 

PROVIDER: S-EPMC8578324 | biostudies-literature | 2021 Nov

REPOSITORIES: biostudies-literature