Insight into interaction mechanism between theaflavin-3-gallate and α-glucosidase using spectroscopy and molecular docking analysis
Journal of Food Biochemistry, ISSN: 1745-4514, Vol: 45, Issue: 1, Page: e13550
2021
- 21Citations
- 11Captures
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
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Metrics Details
- Citations21
- Citation Indexes21
- 21
- CrossRef3
- Captures11
- Readers11
- 11
Article Description
To elucidate the α-glucosidase (α-GC) inhibitory mechanism of theaflavin-3-gallate (TF-3-G), their interaction mechanism was investigated using spectroscopy and molecular docking analysis. The inhibition ratio of TF-3-G against α-GC was determined to be 92.3%. Steady fluorescence spectroscopy showed that TF-3-G effectively quenched the intrinsic fluorescence of α-GC through static quenching, forming a stable complex through hydrophobic interactions. Formation of the TF-3-G/α-GC complex was also confirmed by resonance light scattering spectroscopy. Synchronous fluorescence spectroscopy and circular dichroism spectroscopy indicated that the secondary structure of α-GC was changed by TF-3-G. Molecular docking was used to simulate TF-3-G/α-GC complex formation, showing that TF-3-G might be inserted into the hydrophobic region around the active site of ɑ-GC, and bind with the catalytic Asp215 and Asp352 residues. The ɑ-GC inhibitory mechanism of TF-3-G was mainly attributed to the change in ɑ-GC secondary structure caused by the complex formation. Practical applications: α-Glucosidase (α-GC) can hydrolyze the glycosidic bonds of starch and oligosaccharides in food and release glucose. Therefore, the inhibition of α-GC activity has been used to treat postprandial hyperglycemia and type 2 diabetes mellitus. Theaflavin-3-gallate (TF-3-G), a flavonoid found in the fermentation products of black tea, exhibits strong inhibition of α-GC activity. However, the α-GC inhibitory mechanism of TF-3-G is unclear. This study aids understanding of this mechanism, and proposed a possibly basic theory for improving the medicinal value of TF-3-G in diabetes therapy.
Bibliographic Details
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=85096676265&origin=inward; http://dx.doi.org/10.1111/jfbc.13550; http://www.ncbi.nlm.nih.gov/pubmed/33150631; https://onlinelibrary.wiley.com/doi/10.1111/jfbc.13550; https://dx.doi.org/10.1111/jfbc.13550; https://onlinelibrary.wiley.com/doi/epdf/10.1111/jfbc.13550
Hindawi Limited
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