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Mechanisms of tannin-induced trypsin inhibition: a molecular approach.
- Source :
-
Langmuir : the ACS journal of surfaces and colloids [Langmuir] 2011 Nov 01; Vol. 27 (21), pp. 13122-9. Date of Electronic Publication: 2011 Sep 29. - Publication Year :
- 2011
-
Abstract
- Association of procyanidins with enzymes has drawn attention over the past few years. This work aimed to bring insights on interaction of the protease trypsin with the procyanidin dimer (B3). This interaction was characterized by fluorescence quenching, saturation transfer difference (STD) NMR, molecular modeling, and through an enzymatic inhibition assay. Further studies were conducted regarding the influence of pectin on the binding process. A general overview of the binding process may be outlined as follows: a) at low procyanidin concentrations (below the critical micellar concentration-(CMC)) a specific interaction probably driven by hydrogen bonds between the protein backbone and the procyanidin occurs and is associated with the reduction of both enzyme activity and fluorescence; b) at high procyanidin concentration (above the CMC) the interaction becomes nonspecific. This variation in both nature and extent of the interaction with the variation of procyanidin concentration shows how tannin self-association may affect the interaction between tannins and proteins. It was also shown that the mechanism through which pectin affects the interaction between procyanidin B3 and trypsin is of a competitive type.
- Subjects :
- Animals
Magnetic Resonance Spectroscopy
Micelles
Molecular Dynamics Simulation
Pectins metabolism
Protein Binding
Protein Conformation
Spectrometry, Fluorescence
Trypsin chemistry
Biflavonoids metabolism
Biflavonoids pharmacology
Catechin metabolism
Catechin pharmacology
Proanthocyanidins metabolism
Proanthocyanidins pharmacology
Trypsin metabolism
Trypsin Inhibitors metabolism
Trypsin Inhibitors pharmacology
Subjects
Details
- Language :
- English
- ISSN :
- 1520-5827
- Volume :
- 27
- Issue :
- 21
- Database :
- MEDLINE
- Journal :
- Langmuir : the ACS journal of surfaces and colloids
- Publication Type :
- Academic Journal
- Accession number :
- 21877746
- Full Text :
- https://doi.org/10.1021/la202280c