Stereoselective binding of an enantiomeric pair of stromelysin-1 inhibitors caused by conformational entropy factors

Isothermal titration calorimetry was used to analyze the binding of an enantiomeric pair of inhibitors to the stromelysin-1 catalytic domain. Differences in binding affinity are attributable to different conformational entropy penalties suffered upon binding. Two possible explanations for these differences are proposed.