Ontology highlight
ABSTRACT:
SUBMITTER: Chaudhary H
PROVIDER: S-EPMC5485007 | biostudies-other | 2017 Jun
REPOSITORIES: biostudies-other
Chaudhary Himanshu H Subramaniam Vinod V Claessens Mireille M A E MMAE
Chemphyschem : a European journal of chemical physics and physical chemistry 20170427 12
The interaction of α-synuclein (αS) with membranes is thought to be critical in the etiology of Parkinson's disease. Besides oligomeric αS aggregates that possibly form membrane pores, the aggregation of αS into amyloid fibrils has been reported to disrupt membranes. The mechanism by which aggregation affects the integrity of membranes is, however, unknown. Here, we show that whereas mature αS fibrils only weakly adhere to POPC/POPG giant unilamellar vesicles (GUVs), fibrillization of αS on the ...[more]