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Spectroscopic detection of β ‐sheet structure in nascent Aβ oligomers
Author(s) -
Wang Mingjuan,
JiJi Renee D.
Publication year - 2011
Publication title -
journal of biophotonics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.877
H-Index - 66
eISSN - 1864-0648
pISSN - 1864-063X
DOI - 10.1002/jbio.201100023
Subject(s) - chemistry , circular dichroism , raman spectroscopy , protein secondary structure , amide , oligomer , peptide , crystallography , beta sheet , spectroscopy , spectral line , resonance (particle physics) , analytical chemistry (journal) , chromatography , polymer chemistry , biochemistry , optics , physics , quantum mechanics , astronomy , particle physics
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. (© 2011 WILEY‐VCH Verlag GmbH & Co. KGaA, Weinheim)