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Stereoselective binding of an enantiomeric pair of stromelysin-1 inhibitors caused by conformational entropy factors.
- Source :
-
Bioorganic & medicinal chemistry letters [Bioorg Med Chem Lett] 2000 Nov 06; Vol. 10 (21), pp. 2427-30. - Publication Year :
- 2000
-
Abstract
- 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.
- Subjects :
- Calorimetry methods
Catalytic Domain
Humans
Matrix Metalloproteinase 3 metabolism
Molecular Conformation
Molecular Structure
Protein Binding
Stereoisomerism
Thermodynamics
Hydroxamic Acids chemistry
Hydroxamic Acids metabolism
Matrix Metalloproteinase Inhibitors
Oligopeptides chemistry
Oligopeptides metabolism
Protease Inhibitors chemistry
Protease Inhibitors metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 0960-894X
- Volume :
- 10
- Issue :
- 21
- Database :
- MEDLINE
- Journal :
- Bioorganic & medicinal chemistry letters
- Publication Type :
- Academic Journal
- Accession number :
- 11078193
- Full Text :
- https://doi.org/10.1016/s0960-894x(00)00495-9