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  • Title: Number of galloyl moiety and intramolecular bonds in galloyl-based polyphenols affect their interaction with alpha-glucosidase.
    Author: Cao J, Yan S, Xiao Y, Han L, Sun L, Wang M.
    Journal: Food Chem; 2022 Jan 15; 367():129846. PubMed ID: 34399273.
    Abstract:
    The inhibition of α-glucosidase by nine galloyl-based polyphenols with free and unfree galloyl moieties (GMs) was studied. The results show that the inhibitory activity increased with the free GM number increasing. For the compounds with unfree GMs, ellagic acid and hexahydroxydiphenoyl group contributed to the enzyme inhibition. Free GMs could bind not only with the active site of α-glucosidase (competitive inhibition character), but also with the non-active sites (uncompetitive one); however, the former binding interaction was stronger than the latter one. All polyphenols that had inhibitory effects quenched α-glucosidase fluorescence in a static mode through forming a polyphenol-enzyme complex. The number of amino acid residues involved in polyphenol-enzyme binding interactions (hydrogen bonding and π-conjugations) increased with the inhibitory activity increasing. Additionally, two polyphenols with 5 free GMs showing certain hypoglycemic effects in maltose-loading test suggests that GM may be an advisable functional factor for alleviation of type II diabetes symptoms.
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