Complexation of peptide with Cu2+ responsible to inducing and enhancing the formation of alpha-helix conformation.
Role of some metal ions on the conformations of peptides was examined by using a series of short alanine-based peptides with single Trp-His (W-H) interaction in different environments. Circular dichroism (CD), Trp (W) fluorescence emission, and Fourier transform infrared (FTIR) spectroscopy revealed that there is a conformational role of Cu2+ in inducing and enhancing the formation of alpha-helix conformation. The complexation of the peptide with Cu2+ is responsible to the conformational effect because the chelation is able to stabilize peptide with an alpha-helix conformation. The possible factors affecting the role of Cu2+ are discussed in the paper. The results in this paper are useful to understand the important structural role of Cu2+ in protein folding and the possible mechanism in some neurodegenerative diseases such as Alzheimer's disease.
Department of Chemistry, Faculty of Science, Konan University, Kobe, Japan.
J
J
Zou
N
N
Sugimoto
D000595:Amino Acid Sequence; D001665:Binding Sites; D002942:Circular Dichroism; D003300:Copper / Q000737:chemistry; D004355:Drug Stability; D066298:In Vitro Techniques; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010455:Peptides / Q000138:chemical synthesis / Q000737:chemistry*; D011485:Protein Binding; D017433:Protein Structure, Secondary; D013050:Spectrometry, Fluorescence; D017550:Spectroscopy, Fourier Transform Infrared
D010455:Peptides; D003300:Copper