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首页> 外文期刊>Biochemistry >Solid-State Nuclear Magnetic Resonance Evidence for an Extended #beta# Strand Conformation of the Membrane-Bound HIV-1 Fusion Peptide
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Solid-State Nuclear Magnetic Resonance Evidence for an Extended #beta# Strand Conformation of the Membrane-Bound HIV-1 Fusion Peptide

机译：膜结合的HIV-1融合肽的扩展＃beta＃链构象的固态核磁共振证据。

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摘要

Solid-state nuclear magnetic resonance (NMR) spectroscopy was applied to the membrane- bound form of a synthetic peptide representing the 23-residue N-terminal fusion peptide domain of the HIV-I gp41 envelope glycoprotein. Ip solid-state NMR line width measurements of singly ~(13)C carbonyl labeled peptides showed that a significant population of the membrane-bound peptide is well-structured in its N-terminal and central regions while the C-terminus has more disorder. There was some dependence of line width on lipid composition, with narrower line widths and hence greater structural order observed for a lipid composition comparable to that found in the virus and its target T cells. In the more ordered N-terminal and central regions of the peptide, the ~(13)C carbonyl chemical shifts are consistent with a nonhelical membrane-bound conformation. Additional evidence for a fJ strand membrane-bound conformation was provided by analysis of 2D rotor-synchronized magic angle spinning NMR spectra of doubly ~(13)C carbonyl labeled peptides. Lipid mixing and aqueous contents leakage assays were applied to demonstrate the fusogenicity of the peptide under conditions comparable to those used for the solid-state NMR sample preparation.
机译：将固态核磁共振（NMR）光谱应用于代表HIV-1 gp41包膜糖蛋白的23-残基N-末端融合肽结构域的合成肽的膜结合形式。单个〜（13）C羰基标记的肽的ip固态NMR线宽测量表明，大量的膜结合肽在其N端和中央区域结构良好，而C端的无序性更大。线宽对脂质组成有一定的依赖性，线宽较窄，因此观察到的脂质组成与病毒及其靶T细胞中的脂质相当，具有更大的结构顺序。在肽的更有序的N末端和中央区域，〜（13）C羰基化学位移与非螺旋膜结合构象一致。通过对双〜（13）C羰基标记的肽进行二维转子同步幻角旋转NMR光谱分析，提供了fJ链膜结合构象的其他证据。进行脂质混合和含水量泄漏测定，以证明在与固态NMR样品制备所用条件相当的条件下，肽具有融合性。

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