CD measurements of β-amyloid (1-40) and (1-42) in the condensed phase

Biopolymers. 2011 Feb;95(2):127-34. doi: 10.1002/bip.21543. Epub 2010 Sep 24.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amyloid beta-Peptides / chemistry*
  • Circular Dichroism / methods
  • Humans
  • In Vitro Techniques
  • Peptide Fragments / chemistry*
  • Protein Multimerization
  • Protein Structure, Quaternary
  • Protein Structure, Secondary

Substances

  • Amyloid beta-Peptides
  • Peptide Fragments
  • amyloid beta-protein (1-40)
  • amyloid beta-protein (1-42)