Linked Life Data

11572974

Source:http://linkedlifedata.com/resource/pubmed/id/11572974

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pubmed-article:11572974pubmed:abstractTextThe HIV-1 gp41 envelope glycoprotein promotes fusion of the virus and cell membranes through the formation of a trimer-of-hairpins structure, in which the amino- and carboxyl-terminal regions of the gp41 ectodomain are brought together. Synthetic peptides derived from these two regions (called N and C peptides, respectively) inhibit HIV-1 entry. In contrast to C peptides, which inhibit in the nanomolar range, N peptides are weak inhibitors with IC(50) values in the micromolar range. To test the hypothesis that the weak inhibition of N peptides results from their tendency to aggregate, we have constructed chimeric variants of the N-peptide region of gp41 in which soluble trimeric coiled coils are fused to portions of the gp41 N peptide. These molecules, which present the N peptide in a trimeric coiled-coil conformation, are remarkably more potent inhibitors than the N peptides themselves and likely target the carboxyl-terminal region of the gp41 ectodomain. The best inhibitors described here inhibit HIV-1 entry at nanomolar concentrations.lld:pubmed
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pubmed-article:11572974pubmed:articleTitleDesign of potent inhibitors of HIV-1 entry from the gp41 N-peptide region.lld:pubmed
pubmed-article:11572974pubmed:affiliationHoward Hughes Medical Institute, Whitehead Institute for Biomedical Research, Department of Biology, Massachusetts Institute of Technology, Nine Cambridge Center, Cambridge, MA 02142, USA.lld:pubmed
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pubmed-article:11572974pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
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