Redox regulation of helical structures in short peptides with an intramolecular ferrocenyl cross-linking agent.
We redox-regulated alpha-helicity of short peptides intramolecularly cross-linked with a ferrocenyl linker between amino acid side chains. The helical content of the cross-linked peptide was estimated to be 56% in the neutral state of the ferrocene core at 25 degrees C. The addition of an oxidant to the solution of the cross-linked peptide enhanced the helicity up to 75%. The increased helical content returned to the same level as that in the previous ferrocene state by further addition of a reductant.
Fujimoto
Kazuhisa
K
Graduate School of Pharmaceutical Sciences, University of Toyama, Sugitani 2630, Toyama 930-0194, Japan. fujimoto@pha.u-toyama.ac.jp
Kawai
Hirokazu
H
Amano
Miwo
M
Inouye
Masahiko
M
D000595:Amino Acid Sequence; D005296:Ferrous Compounds / Q000737:chemistry*; D010084:Oxidation-Reduction; D010455:Peptides / Q000737:chemistry*; D011487:Protein Conformation
D005296:Ferrous Compounds; D010455:Peptides