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.
Parker
M H
MH
University of Alabama at Birmingham, 35294, USA. matthew_parker@vpharm.com
Ortwine
D F
DF
O'Brien
P M
PM
Lunney
E A
EA
Banotai
C A
CA
Mueller
W T
WT
McConnell
P
P
Brouillette
C G
CG
D002151:Calorimetry / Q000379:methods; D020134:Catalytic Domain; D006801:Humans; D006877:Hydroxamic Acids / Q000737:chemistry* / Q000378:metabolism*; D019278:Matrix Metalloproteinase 3 / Q000378:metabolism; D061965:Matrix Metalloproteinase Inhibitors; D008968:Molecular Conformation; D015394:Molecular Structure; D009842:Oligopeptides / Q000737:chemistry* / Q000378:metabolism*; D011480:Protease Inhibitors / Q000737:chemistry* / Q000378:metabolism*; D011485:Protein Binding; D013237:Stereoisomerism; D013816:Thermodynamics
C370242:(R)-2-(4'-bromo-biphenyl-4-sulfonyl-amino)-3-methyl-butyric acid; D006877:Hydroxamic Acids; D061965:Matrix Metalloproteinase Inhibitors; D009842:Oligopeptides; D011480:Protease Inhibitors; D019278:Matrix Metalloproteinase 3