Wasniewski Christopher M, Parkanzky Paul D, Bodner Michele L, Weliky David P
Department of Chemistry, Michigan State University, East Lansing, MI 48824-1322, USA.
Chem Phys Lipids. 2004 Nov;132(1):89-100. doi: 10.1016/j.chemphyslip.2004.09.008.
The human immunodeficiency virus (HIV) and influenza virus fusion peptides are approximately 20-residue sequences which catalyze the fusion of viral and host cell membranes. The orientations of these peptides in lipid bilayers have been probed with 15N solid-state nuclear magnetic resonance (NMR) spectroscopy of samples containing membranes oriented between stacked glass plates. Each of the peptides adopts at least two distinct conformations in membranes (predominantly helical or beta strand) and the conformational distribution is determined in part by the membrane headgroup and cholesterol composition. In the helical conformation, the 15N spectra suggest that the influenza peptide adopts an orientation approximately parallel to the membrane surface while the HIV peptide adopts an orientation closer to the membrane bilayer normal. For the beta strand conformation, there appears to be a broader peptide orientational distribution. Overall, the data suggest that the solid-state NMR experiments can test models which correlate peptide orientation with their fusogenic function.
人类免疫缺陷病毒（HIV）和流感病毒的融合肽是大约由20个氨基酸残基组成的序列，可催化病毒膜与宿主细胞膜的融合。通过对夹在堆叠玻璃板之间的定向膜样品进行15N固态核磁共振（NMR）光谱分析，探究了这些肽在脂质双层中的取向。每种肽在膜中至少采用两种不同的构象（主要是螺旋或β链），其构象分布部分由膜头基团和胆固醇组成决定。在螺旋构象中，15N光谱表明流感肽采取的取向大致平行于膜表面，而HIV肽采取的取向更接近膜双层法线。对于β链构象，肽的取向分布似乎更广泛。总体而言，数据表明固态NMR实验可以检验将肽取向与其融合功能相关联的模型。
