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The substitution sites of hydroxyl and galloyl groups determine the inhibitory activity of human pancreatic α-amylase in twelve tea polyphenol monomers

Lan Zhang, Haocun Kong, Bimal Chitrakar, Xiaofeng Ban, Zhengbiao Gu, Yan Hong, Li Cheng, Zhaofeng Li, Caiming Li

2024International Journal of Biological Macromolecules12 citationsDOI

Topics & Concepts

PolyphenolChemistryTheaflavinIC50Docking (animal)Mixed inhibitionInhibitory postsynaptic potentialStereochemistryAmylaseQuantitative structure–activity relationshipGallateBiochemistryEnzymeAntioxidantNon-competitive inhibitionIn vitroBiologyNeuroscienceNursingMedicineNuclear chemistryNatural Antidiabetic Agents StudiesEnzyme Production and CharacterizationAdvanced Glycation End Products research
The substitution sites of hydroxyl and galloyl groups determine the inhibitory activity of human pancreatic α-amylase in twelve tea polyphenol monomers | Litcius