66102-32-7Relevant articles and documents
Long-range electron transfer in rigid 310-helical oligopeptides containing redox cyclic α-amino acids
Lang, Kamil,Kuki, Atsuo
, p. 579 - 584 (1999)
Intrahelical photoinduced electron transfer processes (ET) in conformationally restricted oligopeptides have been studied by nanosecond time-resolved transient spectroscopy. The helical peptides were constructed from sterically hindered α-aminoisobutyric acid (Aib) and two cyclic α-amino acids (Aib class) bearing electron acceptor and donor side chains (DkNap, ThQx). This helical backbone design provides high conformation stability, as previously demonstrated, and yields reliable 310-helical architectures in solution. The forward ET between ThQx and 3DkNap is followed by a slow back ET thus giving rise to an accumulation of the charge-separated ion pairs for hundreds of nanoseconds. We demonstrate the modulation of electronic interactions by the number of intervening Aib residues separating acceptor-donor side chains and propose modifications of the peptide framework by inclusion of a non-Aib amino acid residue. These well-defined and sterically stable frameworks are suited for the precise evaluation of intrahelical electron transfer processes mediated by peptides.