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Peptides trap HIV-1 envelope glycoprotein fusion intermediate at two sites.

Vaccine Weekly

| March 12, 2003 | COPYRIGHT 2003 NewsRX. This material is published under license from the publisher through the Gale Group, Farmington Hills, Michigan.  All inquiries regarding rights should be directed to the Gale Group. (Hide copyright information)Copyright

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 ...

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Source: HighBeam Research, Peptides trap HIV-1 envelope glycoprotein fusion intermediate at two...

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