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Epigallocatechin 3-gallate Binds to Human Salivary α-Amylase with Complex Hydrogen Bonding Interactions

Authors :
Jee-Young Lee
Ki-Woong Jeong
Yangmee Kim
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.

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