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首页> 外文期刊>The journal of physical chemistry, B. Condensed matter, materials, surfaces, interfaces & biophysical >Behavior of Water Near Multimodal Chromatography Ligands and Its Consequences for Modulating Protein-Ligand Interactions
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Behavior of Water Near Multimodal Chromatography Ligands and Its Consequences for Modulating Protein-Ligand Interactions

机译：多式色谱法附近水的行为及其调节蛋白质 - 配体相互作用的后果

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摘要

Multimodal chromatography is a powerful approach for purifying proteins that uses ligands containing multiple modes of interaction. Recent studies have shown that selectivity in multimodal chromatographic separations is a function of the ligand structure and geometry. Here, we performed molecular dynamics simulations to explore how the ligand structure and geometry affect ligand-water interactions and how these differences in solution affect the nature of protein-ligand interactions. Our investigation focused on three chromatography ligands: Capto MMC, Nuvia cPrime, and Prototype 4, a structural variant of Nuvia cPrime. First, the solvation characteristics of each ligand were quantified via three metrics: average water density, fluctuations, and residence time. We then explored how solvation was perturbed when the ligand was bound to the protein surface and found that the probability of the phenyl ring dewetting followed the order: Capto MMC > Prototype 4 > Nuvia cPrime. To explore how these differences in dewetting affect protein-ligand interactions, we calculated the probability of each ligand binding to different types of residues on the protein surface and found that the probability of binding to a hydrophobic residue followed the same order as the dewetting behavior. This study illustrates the role that wetting and dewetting play in modulating protein-ligand interactions.
机译：多模式色谱法是一种利用含有多种相互作用模式的配体纯化蛋白质的有效方法。最近的研究表明，多峰色谱分离的选择性是配体结构和几何形状的函数。在这里，我们进行了分子动力学模拟，以探索配体结构和几何形状如何影响配体-水相互作用，以及溶液中的这些差异如何影响蛋白质-配体相互作用的性质。我们的研究集中在三种色谱配体上：Capto-MMC、Nuvia cPrime和Nuvia cPrime的结构变体Prototype 4。首先，通过三个指标量化每个配体的溶剂化特性：平均水密度、波动和停留时间。然后，我们探索了当配体结合到蛋白质表面时，溶剂化是如何受到干扰的，并发现苯环脱湿的可能性遵循以下顺序：Capto MMC>Prototype 4>Nuvia cPrime。为了探索脱湿差异如何影响蛋白质-配体相互作用，我们计算了每个配体与蛋白质表面不同类型残基结合的概率，发现与疏水残基结合的概率与脱湿行为的顺序相同。这项研究阐明了润湿和去湿在调节蛋白质-配体相互作用中的作用。

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