Epand R M, Cheetham J J, Epand R F, Yeagle P L, Richardson C D, Rockwell A, Degrado W F
Department of Biochemistry, McMaster University Health Sciences Centre, Hamilton, Ontario, Canada.
Biopolymers. 1992 Apr;32(4):309-14. doi: 10.1002/bip.360320403.
The fusion of enveloped viruses to target membranes is promoted by certain viral fusion proteins. However, many other proteins and peptides stabilize bilayer membranes and inhibit membrane fusion. We have evaluated some characteristics of the interaction of peptides that are models of segments of measles and influenza fusion proteins with membranes. Our results indicate that these models of the fusogenic domains of viral fusion proteins promote conversion of model membrane bilayers to nonbilayer phases. This is opposite to the effects of peptides and proteins that inhibit viral fusion. A peptide model for the fusion segment of the HA protein of influenza increased membrane leakage as well as promoted the formation of nonbilayer phases upon acidification from pH 7-5. We analyze the gross conformational features of the peptides, and speculate on how these conformational features relate to the structures of the intact proteins and to their role in promoting membrane fusion.
某些病毒融合蛋白可促进包膜病毒与靶膜的融合。然而，许多其他蛋白质和肽可稳定双层膜并抑制膜融合。我们评估了一些作为麻疹和流感融合蛋白片段模型的肽与膜相互作用的某些特性。我们的结果表明，这些病毒融合蛋白融合结构域的模型可促进模型膜双层向非双层相的转变。这与抑制病毒融合的肽和蛋白质的作用相反。流感HA蛋白融合片段的肽模型增加了膜泄漏，并在从pH 7酸化至pH 5时促进了非双层相的形成。我们分析了这些肽的总体构象特征，并推测这些构象特征如何与完整蛋白质的结构及其在促进膜融合中的作用相关。
