HIV-1进入抑制剂的研究主要集中在HIV包膜糖蛋白gp120与宿主细胞表面CD4分子和辅助受体的结合位点,以及跨膜糖蛋白gp41的融合活性。细胞表面蛋白质二硫键异构酶可以粘附到受体CD4分子上,并于CD4分子与包膜糖蛋白gp120结合位点临近。这种结合可以分解包膜糖蛋白gp120上的二硫键,进而促使包膜糖蛋白gp120和跨膜蛋白gp41发生主要的构象变化,使HIV进入到宿主细胞。
HIV-1 entry inhibitors researches mainly aim at the binding site of the viral envelope glycoprotein gpl20 and cellular CD4, and co-receptors, or blocking a late stage of the fusogenic activity of adjacent gp41. Protein disulfiide isomerizes (PDI) could attach to the primary receptor CD4 close to the gpl20-binding site. This could reduce gp120 disulfide bonds, which trigger the major conformafional changes in gpl20 and gp41 required for virus entry.