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

Lookup NU author(s): Professor Steve Homans


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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-I) 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.

Publication metadata

Author(s): Malham R, Johnstone S, Bingham RJ, Barratt E, Phillips SEV, Laughton CA, Homans SW

Publication type: Article

Publication status: Published

Journal: Journal of the American Chemical Society

Year: 2005

Volume: 127

Issue: 48

Pages: 17061-17067

ISSN (print): 0002-7863

ISSN (electronic): 1520-5126

Publisher: American Chemical Society


DOI: 10.1021/ja055454g


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