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. 2024 Mar 16:22:101296.
doi: 10.1016/j.fochx.2024.101296. eCollection 2024 Jun 30.

Potential anti-hyperglycemic activity of black tea theaflavins through inhibiting α-amylase

Maiquan Li  1   2 , Yunxia Dong  1 , Mangjun Kang  1 , Tiantian Tao  1 , Wenlan Li  1 , Sheng Zhang  2 , Wei Quan  1 , Zhonghua Liu  2
Affiliations

Potential anti-hyperglycemic activity of black tea theaflavins through inhibiting α-amylase

Maiquan Li et al. Food Chem X. .

Abstract

Hyperglycemia can cause early damage to human bady and develop into diabates that will severely threaten human healthy. The effectively clinical treatment of hyperglycemiais is by inhibiting the activity of α-amylase. Black tea has been reported to show inhibitory effect on α-amylase and can be used for hyperglycemia treatment. However, the mechanism underlying is unclear. In this study, in vivo experiment showed that black tea theaflavins extract (BTE) effectively alleviated hyperglycemia. In vitro experiment showed that the effects may be caused by the interation between theaflavins and α-amylase. While TF1 and TF3 were mixed type inhibitors of α-amylase, TF2A and TF2B were competitive inhibitors of α-amylase. Molecular docking analysis showed that theaflavins monomers interacted with the hydrophobic region of α-amylase. Further study verified that monomer-α-amylase complex was spontaneously formed depending on hydrophobic interactions. Taken together, theaflavins showed potential anti-hyperglycemia effect via inhibiting α-amylase activity. Our results suggested that theaflavins might be utilized as a new type of α-amylase inhibitor to prevent and cure hyperglycemia.

Keywords: Black tea; Hypoglycemic activity; Interaction mechanism; Theaflavins; α-amylase.

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Conflict of interest statement

We declare that we have no financial and personal relationships with other people or organizations that can inappropriately influence our work, there is no professional or other personal interest of any nature or kind in any product service and/or company that could be construed as influencing the position presented in the manuscript.

Figures

Unlabelled Image
Graphical abstract
Fig. 1
Fig. 1
Timeline depicting the diet of BTE or ad libitum in each group.
Fig. 2
Fig. 2
Effect of the BTE on STZ-induced diabetic mice. Control: normal control group were fed ad libitum. Model: The diabetic mice induced by STZ were fed ad libitum. PC: STZ-induced diabetic mice were fed ad libitum and oral gavage with glipalamide 20 mg/kg/d. BTE: STZ-induced diabetic mice were fed ad libitum and oral gavage with BTE 200 mg/kg/d. ##: p < 0.01 versus Control. **; p < 0.01 versus Model.
Fig. 3
Fig. 3
The inhibition effects of BTE and theaflavins monomers on α-amylase. a: BTE; b: Acarbose; c:TF1; d:TF2A; e:TF2B; f:TF3.
Fig. 4
Fig. 4
The double-reciprocal Lineweaver-Burk plot analysis for the inhibition of α-amylase against theaflavins monomers. a:TF1; b:TF2A; c:TF2B; d:TF3.
Fig. 5
Fig. 5
The image of the interaction obtained after the docking of TF1(a), TF2A(b), TF2B(c), TF3(d) with α-amylase.
Fig. 6
Fig. 6
Ultraviolet-Visible absorption spectra of theaflavins monomer-α-amylase system. a:TF1; b:TF2A; c:TF2B; d: TF3.
Fig. 7
Fig. 7
Fluorescence spectrum of α-amylase (10u/mL) with different concentrations of theaflavins monomer at 298 K, 303 K, 310 K. a:TF1; b:TF2A; c:TF2B; d: TF3.
See this image and copyright information in PMC

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