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Strong solute-solute dispersive interactions in a protein-ligand complex
Richard Malham1, Sarah Johnstone, Richard J Bingham
1Astbury Centre for Structural Molecular Biology, School of Biochemistry & Molecular Biology, University of Leeds, UK.
Journal of the American Chemical Society
|December 1, 2005
Summary
Dispersion interactions between solutes and proteins are significant for binding thermodynamics, challenging previous assumptions. These interactions, not the hydrophobic effect, drive the binding of primary alcohols to major urinary protein-1.
Area of Science:
- Biochemistry
- Chemical Physics
- Molecular Interactions
Background:
- Solute-solute dispersion interactions were previously underestimated in binding thermodynamics.
- This assumption stemmed from the perceived balance between solute-solvent and solute-solute dispersion interactions.
Purpose of the Study:
- To investigate the role of solute-solute dispersion interactions in protein-ligand binding.
- To re-evaluate the contribution of dispersion forces versus the hydrophobic effect in binding thermodynamics.
Main Methods:
- Thermodynamic analysis of primary alcohol binding to major urinary protein-1 (MUP-I).
- Examining the enthalpy and entropy changes associated with ligand binding.
Main Results:
- Binding thermodynamics showed a linear dependence of enthalpy and entropy on alcohol chain length.
- Enthalpy became more favorable, while entropy became less favorable with increasing chain length.
- Dispersion interactions between the ligand and MUP-I were identified as the primary drivers of binding.
Conclusions:
- The assumption of negligible solute-solute dispersion interactions is not universally justified.
- Ligand-protein dispersion interactions play a crucial role in the binding of primary alcohols to MUP-I.
- Binding is primarily driven by favorable dispersion interactions, not the classical hydrophobic effect.
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