Strong Solute-Solute Dispersive Interactions in a Protein-Ligand Complex

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• 作者：Richard Malham ; Sarah Johnstone ; Richard J. Bingham ; Elizabeth Barratt ; Simon E. V. Phillips ; Charles A. Laughton ; and Steve W. Homans
• 刊名：Journal of the American Chemical Society
• 出版年：2005
• 出版时间：December 7, 2005
• 年：2005
• 卷：127
• 期：48
• 页码：17061 - 17067
• 全文大小：359K
• 年卷期：v.127,no.48(December 7, 2005)
• ISSN：1520-5126

文摘

The contributions of solute-solute dispersion interactions to binding thermodynamics havegenerally been thought to be small, due to the surmised equality between solute-solvent dispersioninteractions 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-I) indicate that thisgeneral assumption is not justified. The enthalpy of binding becomes more favorable with increasing chainlength, whereas the entropy of binding becomes less favorable, both parameters showing a lineardependence. Despite the hydrophobicity of the interacting species, these data show that binding is notdominated by the classical hydrophobic effect, but can be attributed to favorable ligand-protein dispersioninteractions.