Liu Shuwen, Zhao Qian, Jiang Shibo
Lindsley F. Kimball Research Institute, New York Blood Center, New York, NY 10021, USA.
Peptides. 2003 Sep;24(9):1303-13. doi: 10.1016/j.peptides.2003.07.013.
Triggered by receptor binding of gp120, the human immunodeficiency virus type 1 (HIV-1) gp41 changes its conformation to a fusogenic six-helix bundle structure. In the present study, this core conformation modeled by the peptides derived from the gp41 N- and C-terminal heptad repeat regions was determined by fluorescence native polyacrylamide gel electrophoresis and size exclusion high-performance liquid chromatography (HPLC). Two previously described small molecule HIV-1 fusion inhibitors significantly blocked the six-helix bundle formation. It suggests that these biophysical techniques can be used in a novel way to study the conformational change of gp41 during virus entry into cells and to identify HIV-1 fusion inhibitors.
在1型人类免疫缺陷病毒（HIV-1）的gp120与受体结合的触发下，HIV-1的gp41会改变其构象，形成具有融合活性的六螺旋束结构。在本研究中，通过荧光天然聚丙烯酰胺凝胶电泳和尺寸排阻高效液相色谱法（HPLC），确定了由gp41 N端和C端七肽重复区域衍生的肽模拟的这种核心构象。两种先前描述的小分子HIV-1融合抑制剂显著阻断了六螺旋束的形成。这表明这些生物物理技术可以以一种新的方式用于研究病毒进入细胞过程中gp41的构象变化，并鉴定HIV-1融合抑制剂。
