食品与发酵工业 >

2024 , Vol. 50 >Issue 10: 134 - 140

DOI: https://doi.org/10.13995/j.cnki.11-1802/ts.036611

研究报告

芦荟大黄素对α-葡萄糖苷酶的抑制作用及机理

  • 潘若瑶 ,
  • 任国艳 ,
  • 马富利 ,
  • 彭琪越 ,
  • 杜鹂莹
展开
  • 1(河南科技大学 食品与生物工程学院,河南 洛阳,471000)
    2(河南省食品原料工程研究中心,河南 洛阳,471000)
    3(国家实验食品加工与安全教育示范中心,河南 洛阳,471000)
第一作者:硕士研究生(任国艳教授为通信作者,E-mail:renguoyan@163.com)

收稿日期: 2023-06-29

  修回日期: 2023-07-14

  网络出版日期: 2024-06-11

基金资助

河南省重点科技攻关项目(182102110345)

收起

Inhibitory effect and mechanism of aloe-emodin on α-glucosidase

  • PAN Ruoyao ,
  • REN Guoyan ,
  • MA Fuli ,
  • PENG Qiyue ,
  • DU Liying
Expand
  • 1(College of Food and Bioengineering, Henan University of Science and Technology, Luoyang 471000, China)
    2(Henan Engineering Research Center of Food Material, Luoyang 471000, China)
    3(National Demonstration Center for Experimental Food Processing and Safety Education, Luoyang 471000, China)

Received date: 2023-06-29

  Revised date: 2023-07-14

  Online published: 2024-06-11

Fold

摘要

抑制α-葡萄糖苷酶活性是控制机体血糖平衡的有效途径。该文通过酶活性实验、紫外光谱法、荧光光谱法、傅里叶变换红外光谱和分子对接等方法研究了芦荟大黄素(aloe-emodin, AE)对α-葡萄糖苷酶的抑制作用及机理。结果表明,AE对α-葡萄糖苷酶活性有显著抑制作用[IC50=(0.031±0.001) mg/mL],抑制类型为混合型抑制。AE通过一个结合位点与酶结合,使酶中的荧光基团发生静态猝灭。AE改变了酶的构象,使酶的α-螺旋、β-转角含量降低,β-折叠、无规则卷曲含量增加。分子对接深入分析结果显示,AE与Thr290、Leu297、Glu296和Asn2592形成氢键,与Leu297等形成范德华力。AE通过这些分子间作用力结合到α-葡萄糖苷酶的疏水结合腔内,改变了酶的构象,使酶活性降低。

关键词： 芦荟大黄素; α-葡萄糖苷酶; 抑制作用; 光谱; 分子对接

本文引用格式

潘若瑶 , 任国艳 , 马富利 , 彭琪越 , 杜鹂莹 . 芦荟大黄素对α-葡萄糖苷酶的抑制作用及机理[J]. 食品与发酵工业, 2024 , 50(10) : 134 -140 . DOI: 10.13995/j.cnki.11-1802/ts.036611

Abstract

Inhibition of α-glucosidase activity is an effective way to control blood glucose balance.The inhibitory effect of aloe emodin (AE) on α-glucosidase and its mechanism were studied by enzyme activity inhibition experiment, ultraviolet spectroscopy, fluorescence spectrometry, Fourier transform infrared spectroscopy, and molecular docking.Results showed that AE had a significant inhibitory effect on α-glucosidase activity [(IC50=(0.031±0.001) mg/mL)], and the inhibitory type was mixed inhibition.AE bound to α-glucosidase with a binding site by static quenching mechanism.The interaction of AE and α-glucosidase changed the conformation of α-glucosidase, resulting in a decrease in the α-helix, β-turn content and an increase in the β-sheet and random coil content.Further analysis by molecular docking showed that AE formed hydrogen bonds with Thr290, Leu297, Glu296, and Asn2592, formed van der Waals forces with Leu297.AE bound to the hydrophobic binding cavity of α-glucosidase by these intermolecular forces, changing the conformation of the enzyme and reducing enzyme activity.

Key words： aloe-emodin; α-glucosidase; inhibition; spectroscopy; molecular docking

参考文献

[1] NAEMI R, SHAHMORADI L.Global experience of diabetes registries:A systematic review[J].Advances in Experimental Medicine and Biology, 2021, 1307:441-455.
[2] 曹维, 金杜欣, 刘瑞, 等.食源性黄酮通过肠道菌群调节II型糖尿病的作用机制研究进展[J].食品与发酵工业, 2024,50(2):372-378.
CAO W, JIN D X, LIU R, et al, Research progress on the mechanism of food-derived flavonoids regulating type II diabetes mellitus via gut microbiota[J].Food and Fermentation Industries, 2024,50(2):372-378.
[3] GRUNBERGER G.Should side effects influence the selection of antidiabetic therapies in type 2 diabetes?[J].Current Diabetes Reports, 2017, 17(4):21.
[4] AMPARO T R, DJEUJO F M, DA SILVA D, et al.New potential use of Protium spruceanum in hyperglycemia:α-Glucosidase inhibition and protection against oxidative stress[J].Journal of the Brazilian Chemical Society, 2021, 32:1988-1996.
[5] PANI A, BARATTA F, PASTORI D, et al.Prevention and management of type II diabetes chronic complications:The role of polyphenols[J].Current Medicinal Chemistry, 2022, 29(6):1099-1109.
[6] ABDELLATEF A A, FATHY M, MOHAMMED A E S I, et al.Inhibition of cell-intrinsic NF-κB activity and metastatic abilities of breast cancer by aloe-emodin and emodic-acid isolated from Asphodelus microcarpus[J].Journal of Natural Medicines, 2021, 75(4):840-853.
[7] PÉREZ Y Y, JIMÉNEZ-FERRER E, ZAMILPA A, et al.Effect of a polyphenol-rich extract from aloe vera gel on experimentally induced insulin resistance in mice[J].The American Journal of Chinese Medicine, 2007, 35(6):1037-1046.
[8] 姚芬. 柿单宁对淀粉消化特性的影响及其机制研究[D].武汉:华中农业大学, 2017.
YAO F.Study on the effects of persimmon tannin on starch digestibility and its mechanism[D].Wuhan:Huazhong Agricultural University, 2017.
[9] 王梦婷. 杨梅叶原花色素基于调控淀粉消化吸收和肝糖代谢的降血糖作用机制[D].杭州:浙江大学, 2021.
WANG M T.The hypoglycemic mechanism of Ye Yuan anthocyanin in Myrica rubra is based on the regulation of starch digestion and absorption and liver sugar metabolism[D].Hangzhou:Zhejiang University, 2021.
[10] HUANG X, ZHU J X, WANG L, et al.Inhibitory mechanisms and interaction of tangeretin, 5-demethyltangeretin, nobiletin, and 5-demethylnobiletin from citrus peels on pancreatic lipase:Kinetics, spectroscopies, and molecular dynamics simulation[J].International Journal of Biological Macromolecules, 2020, 164:1927-1938.
[11] 曹舒云, 郑瑜雪, 柴子淇, 等.芹菜素-8-C-葡萄糖苷对淀粉消化酶抑制作用机制[J].食品科学, 2023, 44(8):131-136.
CAO S Y, ZHENG Y X, CHAI Z Q, et al.Inhibition mechanism of apigenin-8-c-glucoside on starch digestive enzymes[J].Food Science, 2023, 44(8):131-136.
[12] NAN G J, SUN J, DING M W, et al.Interaction behavior between myricetin and dihydromyricetin with pepsin by spectroscopic and docking methods[J].Journal of Molecular Liquids, 2016, 223:128-135.
[13] WANG J M, MA L, ZHANG Y H, et al.Investigation of the interaction of deltamethrin (DM) with human serum albumin by multi-spectroscopic method[J].Journal of Molecular Structure, 2017, 1129:160-168.
[14] ZHENG Y X, TIAN J H, YANG W H, et al.Inhibition mechanism of ferulic acid against α-amylase and α-glucosidase[J].Food Chemistry, 2020, 317:126346.
[15] ZENG L, DING H F, HU X, et al.Galangin inhibits α-glucosidase activity and formation of non-enzymatic glycation products[J].Food Chemistry, 2019, 271:70-79.
[16] SUN L J, CHEN W Q, MENG Y H, et al.Interactions between polyphenols in thinned young apples and porcine pancreatic α-amylase:Inhibition, detailed kinetics and fluorescence quenching[J].Food Chemistry, 2016, 208:51-60.
[17] ĆORKOVIĆ I, GAŠO-SOKAČ D, PICHLER A, et al.Dietary polyphenols as natural inhibitors of α-amylase and α-glucosidase[J].Life, 2022, 12(11):1692.
[18] 梁宗瑶, 魏园园, 任维维, 等.橡子仁萃取物成分分析及对α-淀粉酶、α-葡萄糖苷酶的抑制作用[J].食品工业科技, 2021, 42(17):47-55.
LIANG Z Y, WEI Y Y, REN W W, et al.Composition analysis and inhibitory effect against α-amylase and α-glucosidase of acorn kernel extractions[J].Science and Technology of Food Industry, 2021, 42(17):47-55.
[19] WANG M T, JIANG J, TIAN J H, et al.Inhibitory mechanism of novel allosteric inhibitor, Chinese bayberry (Myrica rubra Sieb.et Zucc.) leaves proanthocyanidins against α-glucosidase[J].Journal of Functional Foods, 2019, 56:286-294.
[20] FEI Q Q, GAO Y, ZHANG X, et al.Effects of Oolong tea polyphenols, EGCG, and EGCG3” Me on Pancreatic α-amylase activity in vitro[J].Journal of Agricultural and Food Chemistry, 2014, 62(39):9507-9514.
[21] HEIBATI-GOOJANI F, FARHADIAN S, SHAREGHI B, et al.Insights into the binding mechanism of putrescine on α-amylase by multiple spectroscopic techniques and molecular docking[J].Journal of Molecular Structure, 2021, 1242:130702.
[22] CAI X, YU J N, XU L M, et al.The mechanism study in the interactions of sorghum procyanidins trimer with porcine pancreatic α-amylase[J].Food Chemistry, 2015, 174:291-298.
[23] HAN L, FANG C, ZHU R X, et al.Inhibitory effect of phloretin on α-glucosidase:Kinetics, interaction mechanism and molecular docking[J].International Journal of Biological Macromolecules, 2017, 95:520-527.
[24] LIN M Z, CHAI W M, ZHENG Y L, et al.Inhibitory kinetics and mechanism of rifampicin on α-glucosidase:Insights from spectroscopic and molecular docking analyses[J].International Journal of Biological Macromolecules, 2019, 122:1244-1252.
[25] REN G Y, SUN H, GUO J Y, et al.Molecular mechanism of the interaction between resveratrol and trypsin via spectroscopy and molecular docking[J].Food & Function, 2019, 10(6):3291-3302.
[26] PAUL B K, GHOSH N, MUKHERJEE S.Binding interaction of a prospective chemotherapeutic antibacterial drug with β-lactoglobulin:Results and challenges[J].Langmuir, 2014, 30(20):5921-5929.
[27] DAI T T, CHEN J, LI Q, et al.Investigation the interaction between procyanidin dimer and α-amylase:Spectroscopic analyses and molecular docking simulation[J].International Journal of Biological Macromolecules, 2018, 113:427-433.
[28] LI Y B, LIU X L, ZHOU H Y, et al.Inhibitory mechanism of engeletin against α-glucosidase[J].Natural Product Communications, 2021, 16(1):1934578X2098672.
[29] HUANG Q, CHAI W M, MA Z Y, et al.Inhibition of α-glucosidase activity and non-enzymatic glycation by tannic acid:Inhibitory activity and molecular mechanism[J].International Journal of Biological Macromolecules, 2019, 141:358-368.
[30] ZHANG C, ZHANG G W, LIAO Y J, et al.Myricetin inhibits the generation of superoxide anion by reduced form of xanthine oxidase[J].Food Chemistry, 2017, 221:1569-1577.
[31] AVWIOROKO O J, ANIGBORO A A, OTUECHERE C A, et al.α-Amylase inhibition, anti-glycation property and characterization of the binding interaction of citric acid with α-amylase using multiple spectroscopic, kinetics and molecular docking approaches[J].Journal of Molecular Liquids, 2022, 360:119454.
[32] SHEN H Y, WANG J, AO J F, et al.Structure-activity relationships and the underlying mechanism of α-amylase inhibition by hyperoside and quercetin:Multi-spectroscopy and molecular docking analyses[J].Spectrochimica Acta Part A:Molecular and Biomolecular Spectroscopy, 2023, 285:121797.
[33] SEKAR G, SIVAKUMAR A, MUKHERJEE A, et al.Existence of hydroxylated MWCNTs demotes the catalysis effect of amylases against starch degradation[J].International Journal of Biological Macromolecules, 2016, 86:250-261.
[34] ZENG L, ZHANG G W, LIAO Y J, et al.Inhibitory mechanism of morin on α-glucosidase and its anti-glycation properties[J].Food & Function, 2016, 7(9):3 953-3 963.
[35] 王静, 刁翠茹, 王华丽, 等.鼠尾草酸对α-淀粉酶的抑制作用[J].食品科学, 2020, 41(3):12-17.
WANG J, DIAO C R, WANG H L, et al.Inhibitory mechanism of carnosic acid on α-amylase[J].Food Science, 2020, 41(3):12-17.
Options
文章导航

/

〈 〉

技术支持：北京玛格泰克科技发展有限公司