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Epigallocatechin 3-gallate Binds to Human Salivary α-Amylase with Complex Hydrogen Bonding Interactions
- Source :
- Bulletin of the Korean Chemical Society. 32:2222-2226
- Publication Year :
- 2011
- Publisher :
- Korean Chemical Society, 2011.
-
Abstract
- Amylase is a digestive enzyme that catalyses the starch into sugar. It has been reported that the green tea flavonoid (or polyphenols) (-)-epigallocatechin 3-gallate (EGCG) inhibits human salivary -amylase (HSA) and induced anti-nutritional effects. In this study, we performed docking study for seven EGCG-like flavonoids and HSA to understand the interaction mechanism of HSA and EGCG and suggest new possible flavonoid inhibitors of HSA. As a result, EGCG and (-)-epicatechin gallate (ECG) bind to HSA with complex hydrogen bonding interactions. These hydrogen bonding interactions are important for inhibitory activity of EGCG against HSA. We suggested that ECG can be a potent inhibitor of HSA. This study will be helpful to understand the mechanism of inhibition of HSA by EGCG and give insights to develop therapeutic strategies against diabetes.
- Subjects :
- chemistry.chemical_classification
biology
Hydrogen bond
Stereochemistry
Flavonoid
food and beverages
General Chemistry
Gallate
complex mixtures
body regions
chemistry
Biochemistry
Docking (molecular)
Polyphenol
embryonic structures
Digestive enzyme
biology.protein
heterocyclic compounds
Amylase
Salivary α amylase
Subjects
Details
- ISSN :
- 02532964
- Volume :
- 32
- Database :
- OpenAIRE
- Journal :
- Bulletin of the Korean Chemical Society
- Accession number :
- edsair.doi...........75a1b294ac051e02286bbd7495e738a6
- Full Text :
- https://doi.org/10.5012/bkcs.2011.32.7.2222