Inhibition mechanism of different structural polyphenols against α-amylase studied by solid-state NMR and molecular docking

• Published in: International journal of biological macromolecules Vol. 275; no. Pt 2; p. 133757
• Main Authors: Peng, Qiyue, Ma, Yunxiang, Wang, Zhipeng, Wang, Jin
• Format: Journal Article
• Language: English
• Published: Elsevier B.V 01.08.2024
• Subjects: Inhibition mechanism; Molecular docking; Polyphenols; Solid-state NMR; α-Amylase; Polyphenols; Solid-state NMR; α-Amylase; Molecular docking; Inhibition mechanism
• ISSN: 0141-8130; 1879-0003; 1879-0003
• DOI: 10.1016/j.ijbiomac.2024.133757

Polyphenol has the considerable effects for inhibition of digestive enzymes, however, inhibition mechanism of molecular size-dependent polyphenols on enzyme activity is still lacking. Herein, inhibition effect and binding interactions of three different structural polyphenols (catechol, quercetin and hesperidin) on α-amylase were studied. Inhibition assays proved that polyphenols significantly inhibited α-amylase and their effects were increased with their molecular sizes. Hesperidin showed the highest inhibition ability of α-amylase, which was determined as IC50 = 0.43 mg/mL. Fluorescence and FT-IR spectroscopy proved that inter-molecular interactions between polyphenols and α-amylase occurred through non-covalent bonds. Besides, the secondary structure of α-amylase was obviously changed after binding with polyphenols. Inter-molecular interactions were investigated using solid-state NMR and molecular docking. Findings proved that hydrogen bonds and π-π stacking interactions were the mainly inter-molecular interactions. We hope this contribution could provide a theoretical basis for developing some digestive enzyme inhibitors from natural polyphenols. [Display omitted]