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2003 MAR 12 - (NewsRx.com & NewsRx.net) -- Peptides trap the human immunodeficiency virus type 1 envelope glycoprotein fusion intermediate at two sites.
According to recent research from the United States, "Human immunodeficiency virus type 1 (HIV-1) entry into target cells requires folding of two heptad-repeat regions (N-HR and C-HR) of gp41 into a trimer of N-HR and C-HR hairpins, which brings viral and target cell membranes together to facilitate membrane fusion. Peptides corresponding to the N-HR and C-HR of gp41 are potent inhibitors of HIV infection. Here we report new findings on the mechanism of inhibition of a N-HR peptide and compare these data with inhibition by a C-HR peptide."
"Using intact envelope glycoprotein (Env) under fusogenic conditions, we show that the N-HR peptide preferentially binds receptor-activated Env and that CD4 binding is sufficient for triggering conformational changes that allow the peptide to bind Env, results similar to those seen with the C-HR peptide," said Yong He and collaborators at the Food and Drug Administration. "However, activation by both CD4 and chemokine receptors further enhances Env binding by both ...
Source: HighBeam Research, Peptides trap HIV-1 envelope glycoprotein fusion intermediate at two...