A Metallopeptide Assembly of the HIV-1 gp41 Coiled Coil Is an Ideal Receptor in Fluorescence Detection of Ligand Binding

Miriam Gochin, Rodney Kiplin Guy, Martin A. Case

Research output: Contribution to journalArticlepeer-review

31 Scopus citations

Abstract

A stable fragment of the HIV-1 gp41 inner coiled coil has been designed. The addition of a transition-metal ion to bipyridylated gp41 peptides stabilizes the trimeric helical structure of the coiled coil through the formation of an octahedral tris-bipyridyl complex, and removes nonspecific aggregation of the hydrophobic peptide (see picture). The resulting structure recognizes peptides known to bind to the viral coiled coil and was used to develop a simple, useful and sensitive assay to rapidly detect binding of potential fusion-inhibiting drugs.

Original languageEnglish
Pages (from-to)5325-5328
Number of pages4
JournalAngewandte Chemie - International Edition
Volume42
Issue number43
DOIs
StatePublished - Nov 10 2003

Keywords

  • FRET assay
  • Metallopeptides
  • N ligands
  • NMR spectroscopy
  • Viruses

ASJC Scopus subject areas

  • Catalysis
  • Chemistry (all)

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