期刊
JOURNAL OF THE FORMOSAN MEDICAL ASSOCIATION
卷 109, 期 2, 页码 94-105出版社
ELSEVIER TAIWAN
DOI: 10.1016/S0929-6646(10)60029-0
关键词
fusion inhibitor; gp41; HIV-1; peptide; therapeutics
资金
- US National Institutes of Health [R01 AI46221, U19 AI76964]
- Natural Science Foundation of China [30729001, U0832001]
- China Scholarship Council
Human immunodeficiency virus (HIV)-1 infection is initiated by the binding of gp120 envelope glycoprotein to its cell receptor (CD4) and a coreceptor (CXCR4 or CCR5), followed by a series of conformational changes in the gp41 transmembrane subunit. These changes include insertion of fusion peptide into the target cell membrane and association of C-heptad repeat (CHR) peptide with the N-heptad repeat (NHR) trimer, a pre-hairpin fusion intermediate. A stable six-helix bundle core is then formed, bringing the viral envelope and target cell membrane into close proximity for fusion. Peptides derived from the CHR region, such as T20 and C34, inhibit HIV-1 fusion by interacting with the gp41 fusion intermediate. A number of anti-HIV-1 peptides and small molecule compounds targeting the gp41 NHR-trimer have been identified. By combining HIV fusion/entry inhibitors targeting different sites in the gp41 fusion intermediate, a potent synergistic effect takes place, resulting in a potential new therapeutic strategy for the HIV infection/AIDS. Here, we present an overview of the current development of anti-HIV drugs, particularly those targeting the gp41 fusion intermediate. [J Formos Med Assoc 2010;109(2):94-105]
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