Abstract Title:

Inhibitory effect of phloretin onα-glucosidase: Kinetics, interaction mechanism and molecular docking.

Abstract Source:

Int J Biol Macromol. 2016 Nov 25 ;95:520-527. Epub 2016 Nov 25. PMID: 27894824

Abstract Author(s):

Lin Han, Chun Fang, Ruixue Zhu, Qiang Peng, Ding Li, Min Wang

Article Affiliation:

Lin Han


As the aglycone of phloridzin, phloretin belongs to dihydrochalcone with antioxidant, anti-inflammatory and antimicrobial activities. In this study, multispectroscopic techniques and molecular docking analysis were used to investigate the inhibitory activity and mechanisms of phloretin onα-glucosidase. The results showed that phloretin reversibly inhibited α-glucosidase in a mixed-type manner and the value of IC50 was 31.26μgL(-1). The intrinsic fluorescence of α-glucosidase was quenched by the interactions with phloretin through a static quenching mechanism and spontaneously formed phloretin-α-glucosidase complex by the driving forces of van der Waals force and hydrogen bond. Atomic force microscope (AFM) studies and FT-IR measurements suggested that the interactions could change the micro-environments and conformation of the enzymes and the molecular docking analysis displayed the exact binding site of phloretin on α-glucosidase. These results indicated that phloretin is a strong α-glucosidase inhibitor, thus could be contribute to the improvement of diabetes mellitus.

Study Type : In Vitro Study

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