α-Amylase inhibition, anti-glycation property and characterization of the binding interaction of citric acid with α-amylase using multiple spectroscopic, kinetics and molecular docking approaches

Oghenetega J. Avwioroko,Akpovwehwee A. Anigboro,Chiagoziem A. Otuechere,Francis O. Atanu,Oluropo F. Dairo,Temidayo T. Oyetunde,Omotayo B. Ilesanmi,Augustine Apiamu,Akpoyovware S. Ejoh,Damilare Olorunnisola,Moses O. Alfred,Martins O. Omorogie,Nyerhovwo J. Tonukari

Journal of Molecular Liquids（2022）

引用 7|浏览9

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摘要

•Kinetics, fluorescence, UV–Vis, FT-IR, Mol. Docking affirmed α-amylase-CA interaction.•CA inhibited α-amylase activity by a mixed inhibition, Kic < Kiu; with moderate IC50.•AMY intrinsic fluorescence was quenched by CA via static mechanism.•CA binding altered AMY native conformation.•CA suppressed Advanced Glycation End-products (AGEs) formation.

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关键词

α-Amylase inhibition,Citric acid,Anti-glycation,Hyperglycemia,Spectroscopy,Molecular docking

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