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首页> 外文期刊>Biochemistry >VSV Transmembrane Domain (TMD) Peptide Promotes PEG-Mediated Fusion of Lipsomes in a Conformationally Sensitive Fashion
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VSV Transmembrane Domain (TMD) Peptide Promotes PEG-Mediated Fusion of Lipsomes in a Conformationally Sensitive Fashion

机译：VSV跨膜域（TMD）肽以构象敏感的方式促进PEG介导的脂质体融合。

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摘要

Helical instability induced by gly residues in the transmembrane domain (TMD) of G protein, the fusion protein of vesicular stomatitis virus (VSV), was speculated to aid in the later steps of the fusion process, because G protein with ala's substituted for the two TMD gly's was inactive (Cleverley, D.Z., and Lenard, J. (1998) Proc. Natl. Acad. Sci. U.S.A. 95, 3425-30). Here we examine the conformations of synthetic peptides corresponding to fusion-active (GGpep) and inactive (AApep; G's repalced by A's) TMDs by CD spectroscopy, and then their effects on the kinetics of poly(ethyleneglycol) (PEG)-mediated fusion of small unilamellar vesicles. GGpep and AApep both assumed history-dependent, non-interconvertible ordered structures. Both peptides were largely helical under all conditions if derived from trifluoroethanol solutions, and aggregated in a beta-sheet from if derived from acetonitrile solutions. In solvent, detergents or lipid bilayers, GGpep showed a greater range of secondary structural features than did AApep. The two peptides had large but different effects on PEG-mediated fusion. Both enhanced the rate but not the extent of lipid mixing. AApep significantly inhibited the extent of fusion pore formation while GGpep had no effect. The initial rate of fusion was enhanced 6-fold by GGpep and less than 2-fold by AApep. Addition of 5 mol% hexadecane overrode all peptide-induced effects. We suggest that both GGpep and hexadecane promote pore formation by stabilizing the nonlamellar structures in fusion intermediates or initial small pores. AApep, which had fewer nonhelical features in its CD spectrum than GGpep, actually inhibited fusion pore formation.
机译：推测水泡性口炎病毒（VSV）的融合蛋白G蛋白的跨膜结构域（TMD）中的甘氨酸残基引起的螺旋不稳定性有助于融合过程的后续步骤，因为带有ala的G蛋白替代了这两个TMD gly处于非活性状态（Cleverley，DZ和Lenard，J.（1998）美国国家科学院院刊95，3425-30）。在这里，我们通过CD光谱检查对应于融合活性（GGpep）和非活性（AApep; G被A取代）TMD的合成肽的构象，然后研究它们对聚乙二醇（PEG）介导的融合动力学的影响。小单层囊泡。 GGpep和AApep都采用了与历史相关的不可互换的有序结构。如果衍生自三氟乙醇溶液，则两种肽在所有条件下基本上都是螺旋的，如果衍生自乙腈溶液，则两种肽在β-折叠中聚集。在溶剂，去污剂或脂质双层中，GGpep的二级结构特征范围比AApep大。这两种肽对PEG介导的融合有很大但不同的作用。两者都提高了脂质混合的速度，但没有提高混合程度。 AApep显着抑制融合孔形成的程度，而GGpep没有作用。 GGpep将最初的融合速率提高了6倍，而AApep则将其融合率降低了不到2倍。添加5 mol％的十六烷可覆盖所有肽诱导的作用。我们建议GGpep和十六烷都通过稳定融合中间体或初始小孔中的非层状结构来促进孔形成。 AApep的CD光谱中的非螺旋特征比GGpep少，实际上抑制了融合孔的形成。

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