Site-specific modification of α-helical peptides with electron donors and acceptors

Bassil I. Dahiyat, Thomas J. Meade*, Stephen L. Mayo

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

15 Scopus citations

Abstract

We have prepared a histidine containing monomeric α-helical peptide, ETH6 (A2KA4KA2HA6HA4KA 4K) in order to study long-range electron transfer (ET). This peptide was site-specifically labeled with a ruthenium (donor) at one histidine and a second ruthenium (acceptor) at a second histidine located on the same peptide. Both the unlabeled peptide and the singly labeled peptide-metal complex, Ru(bpy)2(im)(His)-ETH6, were shown to form stable monomeric α-helical structures as determined by circular dichroism. Ru(NH3)4(py) was coupled to Ru(bpy)2(im)(His)-ETH6, forming a Ru(bpy)2(im)(His)-ETH6-(His)Ru(NH3)4(py) donor-acceptor complex. The synthesis and characterization of these peptides provide an entry into a series of molecules that are ideally suited to evaluate pathway differences such as H-bond mediated versus backbone-coupled long-range ET in protein α-helices.

Original languageEnglish (US)
Pages (from-to)207-212
Number of pages6
JournalInorganica Chimica Acta
Volume243
Issue number1-2
DOIs
StatePublished - Feb 29 1996

Funding

dation, the David and Lucile Packard Foundation and the Searle Scholars Program. B.I.D. is partially supported by NIH Training Grant GM 08346. T.J.M. acknowledges support from the Petroleum Research Fund, American Chemical Society and the Research Corporation. We thank H. Qian for the computer program implementing Lifson-Roig theory, G. Hathaway for mass spectral analysis and J.F. Kayyem for helpful discussions. S.L.M. acknowledges support from the Rita Allen Foun-

Keywords

  • Electron transfer
  • Ruthenium complexes
  • α-Helical peptides complexes

ASJC Scopus subject areas

  • Physical and Theoretical Chemistry
  • Inorganic Chemistry
  • Materials Chemistry

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