Abstract

Kultida Thongnum and Saksit Chanthai

DOI : http://dx.doi.org/10.13005/ojc/340501

This work aims to investigate the inhibitory activity of capsaicin, which is one of capsaicinoid compounds, on these enzymes using a molecular docking and quantum calculation. Acarbose, a commercial diabetes drug, was also investigated for comparison. The docking results revealed that acarbose yields better inhibition efficiency with binding free energy (ΔG_binding) of about -8.2 to -11.9 kcal/mol, and inhibition constant (K_i) of about 0.0002 to 0.4 µM, whereas capsaicin provided the ΔG_binding of -5.8 to -6.1 kcal/mol and K_i of 23.7 to 45.9 µM. The total binding energy (ΔE_binding) between each inhibitor and amino acids in active site of enzyme obtained from quantum calculation with MP2/6-31G(d,p) level is in agreement with the ΔG_binding, i.e. the ΔE_binding of acarbose was larger negative than that of capsaicin. The amino acids interacting with inhibitor as hydrogen bond mainly contribute to the total binding energy. Nevertheless, it could be concluded that capsaicinoids have high potential to be developed as an alternative drug for diabetes disease.

Antidiabetes; α-Amylase; α-Glucosidase; Capsaicinoids; Molecular Docking, Quantum Calculation

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