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CD measurements of β‐amyloid (1–40) and (1–42) in the condensed phase
Author(s) -
Harada Takunori,
Kuroda Reiko
Publication year - 2011
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.21543
Subject(s) - chemistry , circular dichroism , anisotropy , phase (matter) , amyloid (mycology) , spectroscopy , artifact (error) , crystallography , analytical chemistry (journal) , chromatography , optics , organic chemistry , inorganic chemistry , artificial intelligence , physics , quantum mechanics , computer science
Circular dichroism (CD) spectroscopy of proteins/peptides in thin films can provide valuable information on the structures in the aggregated states; however, it is difficult to estimate the secondary structure content quantitatively due to artifact signals arising from macroscopic anisotropies which is unique to the solid phase. Using a Universal Chiroptical Spectrophotometer (UCS‐1) together with the measurement and analytical procedures we have developed, we could obtain artifact‐free CD spectra of cast and Langmuir‐Blodgett (L‐B) films of synthetic peptides, Aβ (1–40) and (1–42) which are related to Alzheimer's disease. The work gave insights into the mechanisms for structural transformation and amyloid‐like aggregation. © 2010 Wiley Periodicals, Inc. Biopolymers 95: 127–134, 2011.