Structure related α-glucosidase inhibitory activity and molecular docking analyses of phenolic compounds from Paeonia suffruticosa

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题名:	Structure related α-glucosidase inhibitory activity and molecular docking analyses of phenolic compounds from Paeonia suffruticosa
作者:	Chen, Po-Chun;Chen, Po-Chun;Sice, Bongani;Dlamini, Bongani Sicelo;Ch, Chiy-Rong;Chen, Chiy-Rong;郭悅雄;Kuo, Yueh-Hsiung;Shi, Wen-Ling;Shih, Wen-Ling;Li, Yun-Sheng;Lin, Yun-Sheng;Chien-Hsing;Lee, Chien-Hsing;Chang, Chi-I;Chang, Chi-I
贡献者:	醫學暨健康學院醫學檢驗暨生物技術學系
关键词:	Enzymatic activity ●Enzyme inhibition mechanism ●α-glucosidase inhibitor ●Paeonia suffruticosa
日期:	2022-01-01
上传时间:	2023-03-29 02:24:05 (UTC+0)
出版者:	亞洲大學
摘要:	High postprandial hyperglycaemia is an important determinant of the development and progression of type 2 diabetes. Thus, inhibition of key digestive enzymes such as α-amylase and α-glucosidase is considered an efficient approach to control glycaemic levels in diabetics. In search of α-amylase and α-glucosidase inhibitors, the root bark of Paeonia suffruticosa was screened for inhibitors, resulting in the isolation of eleven phenolic compounds (1–11). Their enzymes inhibitory activities and inhibition mechanism were investigated using an in vitro inhibition assay and molecular docking studies. Compounds 2, 5, 6, and 8–11 (IC50 between 290 and 431??M) inhibited α-glucosidase more effectively than the reference compound acarbose (IC50?=?1463.0?±?29.5??M). However, the compounds (IC50?>?800??M) were less effective against α-amylase than acarbose (IC50?=?16.6?±?0.9??M). Among them, compound 10 exhibited the highest α-glucosidase inhibitory effect with an IC50 value of 290.4?±?9.6??M. Compounds 2, 5, 9 10 and 11 were found to be competitive inhibitors, while compounds 6 and 8 were noncompetitive inhibitors of α-glucosidase. Computational analyses showed that the main binding forces between the compounds and the main residues were hydrogen bonds. The results suggest that these compounds have the potential to be developed as α-glucosidase inhibitors.
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