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Strong solute-solute dispersive interactions in a protein-ligand complex.

Malham R, Johnstone S, Bingham RJ, Barratt E, Phillips SE, Laughton CA, Homans SW
J Am Chem Soc 127 17061-7 (2005)
Related entries: 1znd, 1zne, 1zng, 1znk, 1znl

Cited: 42 times
EuropePMC logo PMID: 16316253

Abstract

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.

Articles - 1znh mentioned but not cited (1)

  1. Implicit treatment of solvent dispersion forces in protein simulations. Hassan SA. J Comput Chem 35 1621-1629 (2014)


Reviews citing this publication (9)

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  8. Ligand binding to nucleic acids and proteins: Does selectivity increase with strength? Schneider HJ. Eur J Med Chem 43 2307-2315 (2008)
  9. Forces Driving a Magic Bullet to Its Target: Revisiting the Role of Thermodynamics in Drug Design, Development, and Optimization. Minetti CA, Remeta DP. Life (Basel) 12 1438 (2022)

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  6. The paradoxical thermodynamic basis for the interaction of ethylene glycol, glycine, and sarcosine chains with bovine carbonic anhydrase II: an unexpected manifestation of enthalpy/entropy compensation. Krishnamurthy VM, Bohall BR, Semetey V, Whitesides GM. J Am Chem Soc 128 5802-5812 (2006)
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  8. Fluoroalkyl and alkyl chains have similar hydrophobicities in binding to the "hydrophobic wall" of carbonic anhydrase. Mecinović J, Snyder PW, Mirica KA, Bai S, Mack ET, Kwant RL, Moustakas DT, Héroux A, Whitesides GM. J Am Chem Soc 133 14017-14026 (2011)
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  20. Specific and non-specific protein association in solution: computation of solvent effects and prediction of first-encounter modes for efficient configurational bias Monte Carlo simulations. Cardone A, Pant H, Hassan SA. J Phys Chem B 117 12360-12374 (2013)
  21. High resolution X-ray structures of mouse major urinary protein nasal isoform in complex with pheromones. Perez-Miller S, Zou Q, Novotny MV, Hurley TD. Protein Sci 19 1469-1479 (2010)
  22. The binding cavity of mouse major urinary protein is optimised for a variety of ligand binding modes. Pertinhez TA, Ferrari E, Casali E, Patel JA, Spisni A, Smith LJ. Biochem Biophys Res Commun 390 1266-1271 (2009)
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  32. Water accessibility to the binding cleft as a major switching factor from entropy-driven to enthalpy-driven binding of an alkyl group by synthetic receptors. Matsumoto S, Iwamoto H, Mizutani T. Chem Asian J 5 1163-1170 (2010)


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