ArticlePloS one2015
Investigate the binding of catechins to trypsin using docking and molecular dynamics simulation.
Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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13 citing papers in PubMed, 97 citations in OpenAlex.
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- Plausible computational insights and new atomic-level perspective of epicathechin gallate fromJournal of biomolecular structure & dynamics · 2022Article
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- Epigenetic Modulators as Potential Multi-targeted Drugs Against Hedgehog Pathway for Treatment of Cancer.The protein journal · 2019Article
- Dietary flavonoids inhibit the glycation of lens proteins: implications in the management of diabetic cataract.3 Biotech · 2019Article
- Computational Molecular Docking and X-ray Crystallographic Studies of Catechins in New Drug Design Strategies.Molecules (Basel, Switzerland) · 2018Review
- In Vitro and In Silico Studies of the Molecular Interactions of Epigallocatechin-3-Molecules (Basel, Switzerland) · 2018Review
- Understanding the inhibitory mechanism of tea polyphenols against tyrosinase using fluorescence spectroscopy, cyclic voltammetry, oximetry, and molecular simulations.RSC advances · 2018Article
- Deciphering the binding behavior of flavonoids to the cyclin dependent kinase 6/cyclin D complex.PloS one · 2018Article
- A distance geometry-based description and validation of protein main-chain conformation.IUCrJ · 2017Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
To explore the inhibitory mechanism of catechins for digestive enzymes, we investigated the binding mode of catechins to a typical digestive enzyme-trypsin and analyzed the structure-activity relationship of catechins, using an integration of molecular docking, molecular dynamics simulation and binding free energy calculation. We found that catechins with different structures bound to a conservative pocket S1 of trypsin, which is comprised of residues 189-195, 214-220 and 225-228. In the trypsin-catechin complexes, Asp189 by forming strong hydrogen bonding, and Gln192, Trp215 and Gly216 through hydrophobic interactions, all significantly contribute to the binding of catechins. The number and the position of hydroxyl and aromatic groups, the structure of stereoisomers, and the orientation of catechins in the binding pocket S1 of trypsin all affect the binding affinity. The binding affinity is in the order of Epigallocatechin gallate (EGCG) > Epicatechin gallate (ECG) > Epicatechin (EC) > Epigallocatechin (EGC), and 2R-3R EGCG shows the strongest binding affinity out of other stereoisomers. Meanwhile, the synergic conformational changes of residues and catechins were also analyzed. These findings will be helpful in understanding the knowledge of interactions between catechins and trypsin and referable for the design of novel polyphenol based functional food and nutriceutical formulas.
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