Caffeoyl substitution decreased the binding and inhibitory activity of quinic acid against α-amylase: The reason why chlorogenic acid is a relatively weak enzyme inhibitor
2022
Song, Yi | Li, Wenyue | Yang, Hefei | Peng, Xiaoke | Yang, Xi | Liu, Xuebo | Sun, Lijun
α-Amylase inhibition of chlorogenic acid (CHA) and its component moieties including quinic acid (QA) and caffeic acid (CA) were characterized by IC₅₀, inhibition kinetics, fluorescence quenching, isothermal titration calorimetry, differential scanning calorimetry and molecular docking. QA was found with the highest inhibitory activity in a competitive-mode, and caffeoyl substitution significantly decreased its inhibition but maintained inhibition type. Interestingly, QA hardly quenched α-amylase fluorescence, while CA quenched that significantly without inhibitory activity. This resulted from lack of aromatic ring in QA that can form π-conjugation with α-amylase fluorescent residues. Besides, the binding constant of QA with α-amylase was higher than CHA. Additionally, QA and CA decreased but CHA remained α-amylase thermal stability, indicating that change in α-amylase spatial structure was related with enzyme residue sites involved in interactions with inhibitors, instead of with inhibition effect. Conclusively, caffeoyl substitution decreased α-amylase inhibition of QA through reducing its binding affinity to the enzyme.
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