化学
苯甲酸
IC50型
淀粉酶
羟基化
氢键
酶
对接(动物)
立体化学
体外
戒指(化学)
抑制性突触后电位
生物化学
有机化学
分子
神经科学
护理部
生物
医学
作者
Lei Guan,Haoyuan Long,Fazheng Ren,Yixuan Li,Hao Zhang
出处
期刊:Nutrients
[MDPI AG]
日期:2022-05-05
卷期号:14 (9): 1931-1931
被引量:2
摘要
Phenolic acids are widely found in fruits and vegetables. The inhibitory effect of phenolic acids on α-amylase, a key enzyme for starch digestion, has attracted the attention of researchers. To further investigate the effects of different substituents on the benzene ring of phenolic acid on the inhibition of α-amylase activity, in vitro experiments and molecular docking were used. The structure-activity relationships of 17 phenolic acids with benzoic acid as the parent nucleus were analyzed by determining their half inhibitory concentration (IC50) toward α-amylase. The results showed that 2,3,4-trihydroxybenzoic acid had the strongest inhibitory effect on α-amylase with an IC50 value of 17.30 ± 0.73 mM. According to the structure-activity analysis, the hydroxyl group at the 2-position on the benzene ring had a strong positive effect on the inhibitory activity of α-amylase, while methoxylation at the 2-position and hydroxylation at the 5-position had a negative effect. Molecular docking revealed that hydrogen bonding and hydrophobic interactions were involved in the inhibition, with hydrogen bonding being the primary force. These findings provide a more comprehensive understanding of phenolic acids as inhibitors of α-amylase and provide new ideas for the design of dietary formulations for diabetic patients.
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