Strong solute-solute dispersive interactions in a protein-ligand complex.
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.
Malham
Richard
R
Astbury Centre for Structural Molecular Biology, School of Biochemistry & Molecular Biology, University of Leeds, UK.
Johnstone
Sarah
S
Bingham
Richard J
RJ
Barratt
Elizabeth
E
Phillips
Simon E V
SE
Laughton
Charles A
CA
Homans
Steve W
SW
D000438:Alcohols / Q000737:chemistry* / Q000378:metabolism*; D000818:Animals; D001665:Binding Sites; D002151:Calorimetry; D018360:Crystallography, X-Ray; D008024:Ligands; D051379:Mice; D008958:Models, Molecular; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism*; D013816:Thermodynamics; D014867:Water / Q000737:chemistry / Q000378:metabolism
D000438:Alcohols; D008024:Ligands; D011506:Proteins; C035737:major urinary proteins; D014867:Water