A computational study of cation-π interactions vs salt bridges in aqueous media:: Implications for protein engineering
A computational study of cation-π interactions vs salt bridges in aqueous media:: Implications for protein engineering
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DOI：
10.1021/ja991755c
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发表时间：
2000-02-09
影响因子：
15
通讯作者：
Dougherty, DA
中科院分区：
文献类型：
--
作者：
Gallivan, JP;Dougherty, DA
一个代表性的盐桥与一个代表性的阳离子-π相互作用在水介质中，并在一系列的有机溶剂的能量意义的直接比较，提出使用从头计算电子结构和SM5.42R/HF溶剂化模型的Cramer和Truhlar。阳离子-π相互作用在水中显示出5.5 kcal/mol的井深，显著大于盐桥所见的2.2 kcal/mol。与这一观点相一致的是，蛋白质数据库的一项调查显示，能量显著的阳离子-π相互作用很少完全隐藏在蛋白质中，而是更喜欢暴露在溶剂中。这些结果表明，工程化表面暴露的阳离子-π相互作用可能是增强蛋白质稳定性的新方法。
A direct comparison of the energetic significance of a representative salt bridge vs a representative cation-pi interaction in aqueous media and in a range of organic solvents is presented using ab initio electronic structures and the SM5.42R/HF solvation model of Cramer and Truhlar. The cation-pi interaction shows a well depth of 5.5 kcal/mol in water, significantly larger than the 2.2 kcal/mol seen for the salt bridge. Consistent with this idea, a survey of the Protein Data Bank reveals that energetically significant cation-pi interactions are rarely completely buried within proteins, but prefer to be exposed to solvent. These results suggest that engineering surface-exposed cation-pi interactions could be a novel way to enhance protein stability.