Schanck A, Peuvot J, Brasseur R
Unité de Chimie Physique Moléculaire et de Cristallographie, Université Catholique de Louvain, Louvain-la-Neuve, Belgium.
Biochem Biophys Res Commun. 1998 Sep 8;250(1):12-4. doi: 10.1006/bbrc.1998.9001.
The influence on model membrane organization of a fusion peptide of SIV and of a nonfusogenic mutant of this peptide was examined by molecular modeling and by 31P NMR. The calculated mode of insertion of the fusion peptide shows that it adopts an oblique orientation towards the lipid-water interface and that this fusion peptide induces a destabilization of the bilayer structure of multilamellar vesicles as evidenced by 31P NMR observations. The SIV mutant showing a more vertical insertion into lipid layers is unable to induce nonlamellar structures. This study reinforces the correlation between fusogenic activity, induction of structures not organized in extended bilayers, and calculated mode of insertion of peptides into lipid layers.
通过分子建模和31P核磁共振研究了SIV融合肽及其非融合突变体对模型膜结构的影响。融合肽插入的计算模式表明，它以倾斜方向朝向脂质-水界面，并且这种融合肽会导致多层囊泡双层结构的不稳定，31P核磁共振观察结果证明了这一点。显示出更垂直插入脂质层的SIV突变体无法诱导非双层结构。这项研究加强了融合活性、诱导非延伸双层结构以及肽插入脂质层的计算模式之间的相关性。
