Salt-Induced Membrane-Bound Conformation of the NAC Domain of α-Synuclein Leads to Structural Polymorphism of Amyloid Fibrils.

ABSTRACT: α-Synuclein (αS) interacts with lipid membranes in neurons to form amyloid fibrils that contribute to Parkinson's disease, and its non-amyloid-β component domain is critical in the fibrillation. In this study, the salt (NaCl) effect on the membrane interaction and fibril formation of αS_57-102 peptide (containing the non-amyloid-β component domain) was characterized at the molecular level because the αS_57-102 fibrils exhibited structural polymorphism with two morphologies (thin and thick) in the presence of NaCl but showed one morphology (thin) in the absence of NaCl. The membrane-bound conformation (before fibrillation) of αS_57-102 had two helical regions (first and second) on the membrane regardless of salt, but the length of the first region largely short

SUBMITTER: Imaura R 

PROVIDER: S-EPMC12024755 | biostudies-literature | 2025 Mar

REPOSITORIES: biostudies-literature