%0 Journal Article
%T Inhibition mechanism of different structural polyphenols against α-amylase studied by solid-state NMR and molecular docking.
%A Peng Q
%A Ma Y
%A Wang Z
%A Wang J
%J Int J Biol Macromol
%V 275
%N 0
%D 2024 Aug 8
%M 38986997
%F 8.025
%R 10.1016/j.ijbiomac.2024.133757
%X 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.