Strong solute-solute dispersive interactions in a protein-ligand complex
Strong solute-solute dispersive interactions in a protein-ligand complex
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DOI：
10.1021/ja055454g
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发表时间：
2005-12-07
影响因子：
15
通讯作者：
Homans, SW
中科院分区：
文献类型：
--
作者：
Malham, R;Johnstone, S;Homans, SW
溶质-溶质分散相互作用对结合热力学的贡献通常被认为是小的，这是由于相互作用之前的溶质-溶剂分散相互作用与相互作用之后的溶质-溶质分散相互作用之间的推测相等。伯醇与主要尿蛋白（MUP-1）结合的热力学表明，这种一般假设是不合理的。随着链长的增加，结合的焓变得更有利，而结合的熵变得不那么有利，两个参数都显示出线性依赖性。尽管相互作用物种的疏水性，这些数据表明，结合是不占主导地位的经典的疏水效应，但可以归因于有利的配体-蛋白质分散相互作用。
The contributions of solute-solute dispersion interactions to binding thermodynamics have generally been thought to be small, due to the surmised equality between solute-solvent dispersion interactions prior to the interaction versus solute-solute dispersion interactions following the interaction. The thermodynamics of binding of primary alcohols to the major urinary protein (MUP-1) indicate that this general assumption is not justified. The enthalpy of binding becomes more favorable with increasing chain length, whereas the entropy of binding becomes less favorable, both parameters showing a linear dependence. Despite the hydrophobicity of the interacting species, these data show that binding is not dominated by the classical hydrophobic effect, but can be attributed to favorable ligand-protein dispersion interactions.