title: Spectroscopic detection of β -sheet structure in nascent Aβ oligomers.
abstract: Deep-UV resonance Raman (UVRR) spectroscopy and circular dichroism (CD) were employed to study the secondary structure of Aβ(1-42) in fresh samples with increasing fractions of oligomeric peptide. A feature with a minimum at ~217 nm appeared in CD spectra of samples containing oligomeric Aβ(1-42). UVRR spectra more closely resembled those of disordered proteins. The primary difference between UVRR spectra was the ratio of the 1236 cm(-1) to 1260 cm(-1) amide III peak intensities, which shifted in favor of the 1236 cm(-1) band as the fraction of oligomeric peptide increased.
authors.affiliation: University of Missouri-Columbia, Department of Chemistry, Columbia, Missouri 65211, USA. mingJuan.Wang@ap.rhodia.com
authors.forename: Mingjuan
authors.initials: M
authors.lastname: Wang
authors.forename: Renee D
authors.initials: RD
authors.lastname: Jiji
mesh_terms: D000544:Alzheimer Disease / Q000378:metabolism / Q000473:pathology; D000577:Amides / Q000032:analysis / Q000737:chemistry; D016229:Amyloid beta-Peptides / Q000032:analysis* / Q000737:chemistry; D002942:Circular Dichroism / Q000379:methods*; D006801:Humans; D017433:Protein Structure, Secondary; D013059:Spectrum Analysis, Raman / Q000379:methods*
chemical_list: D000577:Amides; D016229:Amyloid beta-Peptides