Surface enhanced Raman spectroscopy distinguishes amyloid Β-protein isoforms and conformational states.

ABSTRACT: Amyloid β-protein (Aβ) self-association is one process linked to the development of Alzheimer's disease (AD). Aβ peptides, including its most abundant forms, Aβ40 and Aβ42, are associated with the two predominant neuropathologic findings in AD, vascular and parenchymal amyloidosis, respectively. Efforts to develop therapies for AD often have focused on understanding and controlling the assembly of these two peptides. An obligate step in these efforts is the monitoring of assembly state. We show here that surface-enhanced Raman spectroscopy (SERS) coupled with principal component analysis (PCA) readily distinguishes Aβ40 and Aβ42. We show further, through comparison of assembly dependent changes in secondary structure and morphology, that the SERS/PCA approach unambiguously differentiates c

SUBMITTER: Yu X 

PROVIDER: S-EPMC6153385 | biostudies-literature | 2018 Aug

REPOSITORIES: biostudies-literature