Conformational distortion in a fibril-forming oligomer arrests alpha-Synuclein fibrillation and minimizes its toxic effects

Abstract

Chakraborty et al. present biophysical and structural insights into fibril-forming oligomers of alpha-synuclein stabilized by heme. They show that heme targets the His50 residue of the oligomers and locks the protein into a different conformation which leads to non-toxic, non-fibrillating oligomer formation, therefore addressing a very important issue in the field of structure of transient oligomers.