Nanoscale Hyperspectral Imaging of Amyloid Secondary Structures in Liquid

Abnormal aggregation of amyloid-β is a very complex and heterogeneous process. Owing to methodological limitations, the pathway still not fully understood. Herein new approach presented in which secondary structure single aggregates investigated with tip-enhanced Raman spectroscopy (TERS) liquid environment. Clearly resolved TERS signatures amide I III bands enabled detailed analysis molecular at each phase primary also small species on surface fibrils attributed nucleation. Notably, β-sheet rearrangement from antiparallel protofibrils parallel observed. This study allows better understanding Alzheimer's disease etiology methodology can be applied studies other neurodegenerative disorders.