Université de Lyon, INSA de Lyon, CPE Lyon, CNRS UMR 5246 ICBMS, Lyon, Villeurbanne Cedex, France.
J Colloid Interface Sci. 2010 Dec 15;352(2):520-5. doi: 10.1016/j.jcis.2010.08.075. Epub 2010 Sep 17.
The HIV-1 envelope glycoprotein 41 (gp41) undergoes large-scale conformational changes in order to induce the fusion of the virus and cell membranes. Thus, we investigated a possible structure transit at the air-water interface for the tryptophan-rich peptide of gp41 (gp41W). The synthetic peptide (KWASLWNWFNITNWLWYIK), corresponding to gp41W, shows interfacial properties on pure water and Tris buffer at pH 8.5. Isotherm measurements and Brewster angle microscopy (BAM) imaging showed that the behavior of the peptide monolayer was dependent on the subphase composition. A homogenous film was formed on buffer during the peptide monolayer compression, while the appearance of condensed domains on pure water could indicate the oligomerization of gp41W during the surface pressure increase. Polarization modulation infrared reflection absorption spectroscopy (PM-IRRAS) showed that, whatever the subphase, gp41W adopts an α-helix structure at the air-water interface and does not transit for any other structure even at high surface pressures.
HIV-1 包膜糖蛋白 41（gp41）发生大规模构象变化，以诱导病毒和细胞膜融合。因此，我们研究了 gp41 富含色氨酸肽（gp41W）在气-液界面的可能结构转变。与 gp41W 对应的合成肽（KWASLWNWFNITNWLWYIK）在纯水和 pH8.5 的 Tris 缓冲液中显示出界面特性。等温线测量和布鲁斯特角显微镜（BAM）成像表明，肽单层的行为取决于亚相组成。在肽单层压缩过程中，在缓冲液上形成均匀的薄膜，而在纯水上出现凝聚区域可能表明 gp41W 在表面压力增加过程中的寡聚化。偏振调制红外反射吸收光谱（PM-IRRAS）表明，无论亚相如何，gp41W 在气-液界面采用α-螺旋结构，即使在高表面压力下也不会转变为任何其他结构。
