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Abstract Title:

Inhibitory effect of pyrogallol onα-glucosidase: Integrating docking simulations with inhibition kinetics.

Abstract Source:

Int J Biol Macromol. 2018 Jun ;112:686-693. Epub 2018 Feb 6. PMID: 29425876

Abstract Author(s):

Li Zheng, Jinhyuk Lee, Li-Mei Yue, Gyu Tae Lim, Jun-Mo Yang, Zhuo-Ming Ye, Yong-Doo Park

Article Affiliation:

Li Zheng

Abstract:

In this study we conducted serial kinetic studies integrated with computational simulations to judge the inhibitory effect of pyrogallol onα-glucosidase, due to the association between this enzyme and the treatment of type 2 diabetes. As a result, we found that pyrogallol bound to the active site of α-glucosidase, interacting with several key residues, such as ASP68, MET69, TYR71, PHE157, PHE158, PHE177, GLN181, HIS348, ASP349, ASP406, VAL407, ASP408, ARG439, and ARG443, which was predicted by performing a protein-ligand docking simulation. Subsequently, we evaluated the inhibitory effect of pyrogallol on α-glucosidase, and found that it induced a mixed type of inhibition in a reversible and quick-binding manner. The relevantkinetic parameters were evaluated to be: IC=0.72±0.051mM; K=0.37±0.018mM. A tertiary conformational change was synchronized with pyrogallol inhibition and modulation of the shape of the active site was correspondingly observed. Our study provides insight into the functional inhibitory role of pyrogallol, which results from its triple-hydroxyl groups interactingwith the active site of α-glucosidase. We suggest that compounds similar to pyrogallol (phenolic hydroxyl compounds) which target the key residues of the active site of α-glucosidase could be potential agents for α-glucosidase inhibition.

Study Type : In Vitro Study

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