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Persimmon highly galloylated-tannins in vitro mitigated α-amylase and α-glucosidase via statically binding with their catalytic-closed sides and altering their secondary structure elements.

Wei ZhuIbrahim KhalifaRuifeng WangChunmei Li
Published in: Journal of food biochemistry (2020)
Reticence of α-amylase (α-Amy) and α-glucosidase (α-Glu) is needed due to their mitigation potency on the glucose absorption. In this study, the anti-amylolytic effects of persimmon tannins (PT) on α-Amy and α-Glu and their interaction mechanisms were investigated. It was found that PT inhibited α-Amy and α-Glu with the half inhibitory concentration (IC50 ) values of 0.35 and 0.24 mg/ml, respectively. Fluorescence and FT-IR spectrometry results showed that PT could bind to enzymes and alter their conformations. Molecular docking showed that the structural units of PT interacted with the key sites (amino acids Glu233, Asp197, and Asp300) of α-Amy by H-bonds and π-π interactions, while they bound to the residues closed to the active sites of α-Glu. The whole results implied that PT was a promising mitigator of α-Amy and α-Glu. It might help to understand mechanisms of glycemic response inhibition of PT and develop certain therapeutic strategies against diabetes. PRACTICAL APPLICATIONS: α-Amy and α-Glu are the crucial starch digestive enzymes associated with type II diabetes mellitus in humans. Persimmon is an excellent source of bio-functional tannins which potentially mitigate the type II diabetes. This study showed that PT beneficially decreased the action of the carbohydrate digestion-related enzymes, namely α-Amy and α-Glu via interaction simultaneously, which could be used to formulate a functional food and natural medicine.
Keyphrases
  • molecular docking
  • type diabetes
  • glycemic control
  • cardiovascular disease
  • molecular dynamics simulations
  • amino acid
  • climate change
  • metabolic syndrome
  • skeletal muscle
  • blood pressure
  • solid phase extraction