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

  1. Miriam Gochin Prof.1,
  2. Rodney Kiplin Guy2,
  3. Martin A. Case3

Article first published online: 4 NOV 2003

DOI: 10.1002/anie.200352006

Issue

Angewandte Chemie International Edition

Angewandte Chemie International Edition

Volume 42, Issue 43, pages 5325–5328, November 10, 2003

Additional Information

How to Cite

Gochin, M., Kiplin Guy, R. and Case, M. A. (2003), A Metallopeptide Assembly of the HIV-1 gp41 Coiled Coil Is an Ideal Receptor in Fluorescence Detection of Ligand Binding. Angewandte Chemie International Edition, 42: 5325–5328. doi: 10.1002/anie.200352006

Author Information

  1. 1

    Dept. Microbiology, University of the Pacific School of Dentistry, San Francisco, CA 94115, USA, and, Dept. Pharmaceutical Chemistry, University of California, San Francisco, CA 94143, USA, Fax (+1) 415-929-6564

  2. 2

    Dept. Pharmaceutical Chemistry, University of California, San Francisco, CA 94143, USA

  3. 3

    Department of Chemistry, University of Vermont, Burlington, VT 0540

  1. †

    This work was supported by grants from the University-wide AIDS research project of the State of California (to M.G.), the American Foundation for AIDS Research (to M.G.), the National Science Foundation (to M.A.C.) and from the Sandler Research Foundation (to R.K.G).

Publication History

  1. Issue published online: 4 NOV 2003
  2. Article first published online: 4 NOV 2003
  3. Manuscript Received: 30 MAY 2003

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Keywords:

  • FRET assay;
  • metallopeptides;
  • N ligands;
  • NMR spectroscopy;
  • viruses

Graphical Abstract

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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.

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