【摘 要】
:
HIV envelope glycoprotein transmembrane subunit gp41 plays a critical rolein the fusion between viral and target cell membranes.Upon gp120 binding to CD4 an
【机 构】
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Lab of Viral Immunology,Lindsley F.Kimball Research Institute, New York Blood Center, 310 East 67th
【出 处】
:
2006中国天津世界艾滋病日科技会议
论文部分内容阅读
HIV envelope glycoprotein transmembrane subunit gp41 plays a critical rolein the fusion between viral and target cell membranes.Upon gp120 binding to CD4 and a coreceptor (CCR5 or CXCR4),gp41 changes its conformation by forming N-helix trimer between N-heptad repeats (NHRs) and then six-helix bundle between the N-trimer and the Cheptad repeats (CHRs).Peptides derived from the NHR and CHR of gp41 extracellular region have demonstrated potent inhibitory activity on the HIV mediated cell fusion.One of these peptides,T-20,became the first success of a new class of anti-HIV agents,named HIV entry inhibitors.However,a relatively long peptide such as T-20 suffers from several limitations including lack of oral bioavailability and high cost of production.
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