Study of electron transfer in ferrocene-labeled collagen-like peptides.
This study describes the electron transfer (ET) phenomenon through a series of (Pro-Hyp-Gly) repeat units containing collagen mimics. The peptides contain redox-active ferrocene (Fc) and thiol-functionalized cystein (Cys) at the N- and C-terminals, respectively. Peptide films were prepared on gold surfaces and characterized by X-ray photoelectron spectroscopy (XPS), ellipsometry, and Fourier transform-reflection absorption infrared spectroscopy (FT-RAIRS). Electrochemical investigations of the films showed a linear but weakly distance-dependent ET. The importance of H-bonding was realized, and the possibility of a conformationally gated ET mechanism has been discussed.
Dey
Subrata K
SK
Department of Chemistry, Bankura Sammilani College, Kenduadihi, Bankura 722102, WB, India. skdusask@yahoo.ca
Long
Yi-Tao
YT
Chowdhury
Somenath
S
Sutherland
Todd C
TC
Mandal
Himadri S
HS
Kraatz
Heinz-Bernhard
HB
D000595:Amino Acid Sequence; D003094:Collagen / Q000737:chemistry*; D004583:Electrons; D005296:Ferrous Compounds / Q000737:chemistry*; D006046:Gold / Q000737:chemistry*; D000075163:Metallocenes; D010455:Peptides / Q000737:chemistry*
D005296:Ferrous Compounds; D000075163:Metallocenes; D010455:Peptides; D006046:Gold; D003094:Collagen; C004998:ferrocene