| Literature DB >> 20004576 |
Kent D Stewart1, Jeffrey R Huth, Teresa I Ng, Keith McDaniel, Rebecca Newlin Hutchinson, Vincent S Stoll, Renaldo R Mendoza, Edmund D Matayoshi, Robert Carrick, Hongmei Mo, Jean Severin, Karl Walter, Paul L Richardson, Leo W Barrett, Robert Meadows, Steve Anderson, William Kohlbrenner, Clarence Maring, Dale J Kempf, Akhter Molla, Edward T Olejniczak.
Abstract
The ectodomain of HIV-1 gp41 mediates the fusion of viral and host cellular membranes. The peptide-based drug Enfuvirtide(1) is precedent that antagonists of this fusion activity may act as anti HIV-agents. Here, NMR screening was used to discover non-peptide leads against this target and resulted in the discovery of a new benzamide 1 series. This series is non-peptide, low molecular weight, and analogs have activity in a cell fusion assay with EC50 values ranging 3-41microM. Structural work on the gp41/benzamide 1 complex was determined by NMR spectroscopy using a designed model peptide system that mimics an open pocket of the fusogenic form of the protein. Copyright 2009 Elsevier Ltd. All rights reserved.Entities:
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Year: 2009 PMID： 20004576 DOI： 10.1016/j.bmcl.2009.11.076
Source DB: PubMed Journal: Bioorg Med Chem Lett ISSN： 0960-894X Impact factor: 2.823