| Autor: |
Li, Siyuan, Yin, Lin, Yi, Juzhen, Zhang, Li‐Ming, Yang, Liqun |
| Předmět: |
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| Zdroj: |
Journal of Food Biochemistry; Jan2021, Vol. 45 Issue 1, p1-11, 11p |
| Abstrakt: |
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. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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