Study on the Structural Effect of Maltoligosaccharides on Cytochrome c Complexes Stabilities by Native Mass Spectrometry.
Study on the Structural Effect of Maltoligosaccharides on Cytochrome c Complexes Stabilities by Native Mass Spectrometry.
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非变质质谱研究麦芽低聚糖对细胞色素 c 复合物稳定性的结构影响
DOI：
10.1007/s13659-017-0150-x
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发表时间：
2018-03
影响因子：
4.7
通讯作者：
Wang X
中科院分区：
文献类型：
--
作者：
Chi Q;Liu YZ;Wang X
摘要配体和靶向蛋白之间的非共价相互作用对于理解蛋白质的分子机制至关重要。在这项工作中，我们研究了细胞色素 c (Cyt c) 与麦芽低聚糖的相互作用，即麦芽糖 (Mal II)、麦芽三糖 (Mal III)、麦芽四糖 (Mal IV)、麦芽五糖 (Mal V)、麦芽六糖 (Mal VI) 和麦芽七糖 (Mal VII)。使用电喷雾电离质谱 (ESI-MS) 分析，观察到 Cyt c 与麦芽低聚糖配体形成的 1:1 和 1:2 复合物。根据解卷积光谱计算相应的缔合常数。所选寡糖与 Cyt c 的相对结合亲和力的顺序为 Mal III > Mal IV > Mal II > Mal V > Mal VI > Mal VII。结果表明，非共价蛋白复合物的稳定性与结合配体的分子结构密切相关。能够与蛋白质氨基残基形成氢键、静电力或疏水力的相关官能团对于蛋白质复合物的稳定性起着重要作用。此外，配体的空间结构对于与蛋白质结合袋的适当相互作用也至关重要。图形摘要
AbstractNoncovalent interactions between ligands and targeting proteins are essential for understanding molecular mechanisms of proteins. In this work, we investigated the interaction of Cytochrome c (Cyt c) with maltoligosaccharides, namely maltose (Mal II), maltotriose (Mal III), maltotetraose (Mal IV), maltopentaose (Mal V), maltohexaose (Mal VI) and maltoheptaose (Mal VII). Using electrospray ionization mass spetrometry (ESI–MS) assay, the 1:1 and 1:2 complexes formed by Cyt c with maltoligosaccharide ligand were observed. The corresponding association constants were calculated according to the deconvoluted spectra. The order of the relative binding affinities of the selected oligosaccharides with Cyt c were as Mal III > Mal IV > Mal II > Mal V > Mal VI > Mal VII. The results indicated that the stability of noncovalent protein complexes was intimately correlated to the molecular structure of bound ligand. The relevant functional groups that could form H-bonds, electrostatic or hydrophobic forces with protein’s amino residues played an important role for the stability of protein complexes. In addition, the steric structure of ligand was also critical for an appropriate interaction with the binding pocket of proteins.Graphical Abstract