Probing the Cross-β Core Structure of Amyloid Fibrils by Hydrogen−Deuterium Exchange Deep Ultraviolet Resonance Raman Spectroscopy

Abstract

Studying the structure of the amyloid fibril is important for understanding fibrillogenesis at a molecular level. Hydrogen−deuterium exchange deep ultraviolet resonance Raman (DUVRR) spectroscopy combined with advanced statistical analysis allowed for structural characterization of the highly ordered cross-β core of lysozyme fibrils. No inhomogeneous broadening of Raman bands due to various amino acid residues was found that might indicate a sequence-independent structure of the cross-β core. The resolved Raman signature indicated that the antiparallel β-sheet is the dominant secondary structural conformation of the core.