CD measurements of β-amyloid (1-40) and (1-42) in the condensed phase.
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.
Harada
Takunori
T
Japan Science and Technology Agency, ERATO-SORST Kuroda Chiromorphology Team, 4-7-6 Komaba, Meguro-ku, Tokyo 153-0041, Japan.
Kuroda
Reiko
R
D016229:Amyloid beta-Peptides / Q000737:chemistry*; D002942:Circular Dichroism / Q000379:methods; D006801:Humans; D066298:In Vitro Techniques; D010446:Peptide Fragments / Q000737:chemistry*; D055503:Protein Multimerization; D020836:Protein Structure, Quaternary; D017433:Protein Structure, Secondary
D016229:Amyloid beta-Peptides; D010446:Peptide Fragments; C078592:amyloid beta-protein (1-40); C075222:amyloid beta-protein (1-42)