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首页> 外文期刊>The journal of physical chemistry, B. Condensed matter, materials, surfaces, interfaces & biophysical >Molecular Dynamics Study of the Solvation of an α-Helical Transmembrane Peptide by DMSO
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Molecular Dynamics Study of the Solvation of an α-Helical Transmembrane Peptide by DMSO

机译：DMSO溶解α-螺旋跨膜肽的分子动力学研究

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摘要

A 10-ns molecular dynamics study of the solvation of a hydrophobic transmembrane helical peptide in dimethyl sulfoxide (DMSO) is presented. The objective is to analyze how this aprotic polar solvent is able to solvate three groups of amino acid residues (i.e., polar, apolar, and charged) that are located in a stable helical region of a transmembrane peptide. The 25-residue peptide (sMTM7) used mimics the cytoplasmic proton hemichannel domain of the seventh transmembrane segment (TM7) from subunit a of H~+-V-ATPase from Saccharomyces cerevisiae. The three-dimensional structure of peptide sMTM7 in DMSO has been previously solved by NMR spectroscopy. The radial and spatial distributions of the DMSO molecules surrounding the peptide as well as the number of hydrogen bonds between DMSO and the side chains of the amino acid residues involved are extracted from the molecular dynamics simulations. Analysis of the molecular dynamics trajectories shows that the amino acid side chains are fully embedded in DMSO. Polar and positively charged amino acid side chains have dipole-dipole interactions with the oxygen atom of DMSO and form hydrogen bonds. Apolar residues become solvated by DMSO through the formation of a hydrophobic pocket in which the methyl groups of DMSO are pointing toward the hydrophobic side chains of the residues involved. The dual solvation properties of DMSO cause it to be a good membrane-mimicking solvent for transmembrane peptides that do not unfold due to the presence of DMSO.
机译：提出了一个10 ns的分子动力学研究，研究了疏水跨膜螺旋肽在二甲亚砜（DMSO）中的溶解。目的是分析这种非质子极性溶剂如何能够溶解位于跨膜肽的稳定螺旋区中的三组氨基酸残基（即极性，非极性和带电荷）。使用的具有25个残基的肽（sMTM7）模仿了来自酿酒酵母（Saccharomyces cerevisiae）H〜+ -V-ATPase的亚基a的第七个跨膜片段（TM7）的细胞质子质子半通道结构域。 DMSO中sMTM7肽的三维结构先前已通过NMR光谱解析。从分子动力学模拟中提取了肽周围的DMSO分子的径向和空间分布，以及DMSO与所涉及氨基酸残基的侧链之间的氢键数量。分子动力学轨迹分析表明，氨基酸侧链完全嵌入DMSO中。极性和带正电荷的氨基酸侧链与DMSO的氧原子发生偶极-偶极相互作用，并形成氢键。非极性残基通过形成疏水口袋而被DMSO溶解，其中DMSO的甲基指向所涉及残基的疏水侧链。 DMSO的双重溶剂化性质使其成为跨膜肽的良好膜模拟溶剂，而跨膜肽由于存在DMSO而不会展开。

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