Exploring the Inhibitory Mechanism of Res on Α-Amylase and Α-Glucosidase Via Enzymatic Inhibition Assay, Multi-Spectroscopic Analysis and Molecular Docking

对接(动物) 酶抑制 化学 淀粉酶 抑制性突触后电位 机制(生物学) 生物化学 生物 物理 医学 护理部 量子力学 神经科学
作者
Fuli Ma,Guoyan Ren,Mingyi Zhou,Ruoyao Pan,Bin Zhang,Jinling Fan
标识
DOI:10.2139/ssrn.4405914
摘要

Inhibition of α-amylase and α-glucosidase activities to delay the hydrolysis of starch to glucose has been considered as an effective strategy to control hyperglycemia. Resveratrol has been shown to have hypoglycemic effects, but its mechanism of inhibiting α-amylase and α-glucosidase activities remains unclear. The inhibitory effect of resveratrol on starch digestion, α-amylase and α-glucosidase activities and its mechanism were investigated by means of starch digestion experiment, enzyme reaction kinetics, multispectral and molecular docking techniques. Resveratrol can significantly reduce the digestibility of starch by inhibiting the activity of starch digestive enzymes or changing the microstructure of starch. Resveratrol inhibited α-amylase and α-glucosidase significantly, with IC50 values of 47.713 μg mL-1 and 26.825 μg mL-1, respectively. Resveratrol inhibited α-amylase in a competitive manner and α-glucosidase in a non-competitive manner. Uv-vis spectra showed that the microenvironment of α-amylase and α-glucosidase aromatic amino acid residues was changed by the addition of resveratrol. Multiple fluorescence spectra showed that resveratrol interacts with α-glucosidase and α-amylase through static quenching mechanism. The interaction of resveratrol and α-glucosidase and α-amylase is spontaneous with at least one binding site with α-glucosidase and α-amylase. Resveratrol interacts with α-glucosidase mainly through hydrogen bonding and van der Waals forces, but with α-amylase through hydrophobic interaction. The molecular docking results showed that resveratrol was bound to the active center of α-amylase and formed a competitive relationship with the substrate, while resveratrol was bound to the hydrophobic pocket of α-glucosidase. This study provides a new idea for the development of powerful drugs or functional foods containing resveratrol, and provides a new way to improve hyperglycemia.

科研通智能强力驱动
Strongly Powered by AbleSci AI
更新
大幅提高文件上传限制,最高150M (2024-4-1)

科研通是完全免费的文献互助平台,具备全网最快的应助速度,最高的求助完成率。 对每一个文献求助,科研通都将尽心尽力,给求助人一个满意的交代。
实时播报
刚刚
英俊的铭应助科研通管家采纳,获得10
1秒前
爆米花应助瑶瑶采纳,获得10
1秒前
jhb完成签到,获得积分10
4秒前
三叶草发布了新的文献求助10
7秒前
7秒前
federish发布了新的文献求助10
7秒前
紫琉花雨完成签到 ,获得积分10
8秒前
13秒前
14秒前
夜猫放羊完成签到,获得积分10
16秒前
陆小果完成签到,获得积分10
16秒前
无花果应助嗨JL采纳,获得10
18秒前
夜猫放羊发布了新的文献求助30
19秒前
SCISSH发布了新的文献求助10
20秒前
Kabutack完成签到,获得积分10
21秒前
鱼儿会飞完成签到,获得积分10
22秒前
酷波er应助小河ovo采纳,获得10
24秒前
29秒前
韩soso发布了新的文献求助10
30秒前
31秒前
32秒前
33秒前
叉叉茶完成签到 ,获得积分10
33秒前
小河ovo发布了新的文献求助10
34秒前
小李要努力Oo完成签到,获得积分20
35秒前
蒋灵馨完成签到 ,获得积分10
35秒前
37秒前
37秒前
Lumos发布了新的文献求助10
37秒前
可爱的函函应助悦耳晓露采纳,获得10
38秒前
38秒前
靓丽翩跹发布了新的文献求助10
38秒前
fangpiupiu发布了新的文献求助10
39秒前
嗨JL发布了新的文献求助10
40秒前
Ruby完成签到,获得积分10
40秒前
zjj完成签到,获得积分10
42秒前
一蓑烟雨任平生完成签到,获得积分10
42秒前
予城发布了新的文献求助10
43秒前
科研66666完成签到 ,获得积分10
43秒前
高分求助中
Licensing Deals in Pharmaceuticals 2019-2024 3000
Effect of reactor temperature on FCC yield 2000
Very-high-order BVD Schemes Using β-variable THINC Method 1020
PraxisRatgeber: Mantiden: Faszinierende Lauerjäger 800
Near Infrared Spectra of Origin-defined and Real-world Textiles (NIR-SORT): A spectroscopic and materials characterization dataset for known provenance and post-consumer fabrics 610
Mission to Mao: Us Intelligence and the Chinese Communists in World War II 600
Promoting women's entrepreneurship in developing countries: the case of the world's largest women-owned community-based enterprise 500
热门求助领域 (近24小时)
化学 医学 生物 材料科学 工程类 有机化学 生物化学 物理 内科学 纳米技术 计算机科学 化学工程 复合材料 基因 遗传学 催化作用 物理化学 免疫学 量子力学 细胞生物学
热门帖子
关注 科研通微信公众号,转发送积分 3304504
求助须知:如何正确求助?哪些是违规求助? 2938464
关于积分的说明 8488809
捐赠科研通 2612923
什么是DOI,文献DOI怎么找? 1427023
科研通“疑难数据库(出版商)”最低求助积分说明 662889
邀请新用户注册赠送积分活动 647385