{"title":"山茶甙 A 对 α-葡萄糖苷酶的抑制机制:体外和分子模拟研究","authors":"Jinze Jia, Lu Bai, Yuzhen Chen, Benguo Liu","doi":"10.3390/foods13172835","DOIUrl":null,"url":null,"abstract":"α-Glucosidase is an important target for type II diabetes treatment, and the search for natural α-glucosidase inhibitors is currently a hot topic in functional food research. Camellianin A is the main flavonoid in the leaves of Adinandra nitida, but research on its inhibition of α-glucosidase is rarely reported. In view of this, the present study systematically investigated the inhibitory impact of camellianin A on α-glucosidase, combining the fluorescence method and molecular docking to explore their interaction, aiming to reveal the relevant inhibitory mechanism. The results indicated that camellianin A possessed excellent α-glucosidase inhibitory activity (IC50, 27.57 ± 0.59 μg/mL), and van der Waals force and hydrogen bonding dominated the binding process between camellianin A and α-glucosidase, with a binding-site number of 1. A molecular docking experiment suggested that camellianin A formed hydrogen bonding with Glu771, Trp391, Trp710, Gly566, Asp568, and Phe444 of α-glucosidase, consistent with the thermodynamic result. Our result can provide a reference for the development of natural α-glucosidase inhibitors.","PeriodicalId":12386,"journal":{"name":"Foods","volume":null,"pages":null},"PeriodicalIF":4.7000,"publicationDate":"2024-09-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Inhibitory Mechanism of Camellianin A against α-Glucosidase: In Vitro and Molecular Simulation Studies\",\"authors\":\"Jinze Jia, Lu Bai, Yuzhen Chen, Benguo Liu\",\"doi\":\"10.3390/foods13172835\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"α-Glucosidase is an important target for type II diabetes treatment, and the search for natural α-glucosidase inhibitors is currently a hot topic in functional food research. Camellianin A is the main flavonoid in the leaves of Adinandra nitida, but research on its inhibition of α-glucosidase is rarely reported. In view of this, the present study systematically investigated the inhibitory impact of camellianin A on α-glucosidase, combining the fluorescence method and molecular docking to explore their interaction, aiming to reveal the relevant inhibitory mechanism. The results indicated that camellianin A possessed excellent α-glucosidase inhibitory activity (IC50, 27.57 ± 0.59 μg/mL), and van der Waals force and hydrogen bonding dominated the binding process between camellianin A and α-glucosidase, with a binding-site number of 1. A molecular docking experiment suggested that camellianin A formed hydrogen bonding with Glu771, Trp391, Trp710, Gly566, Asp568, and Phe444 of α-glucosidase, consistent with the thermodynamic result. Our result can provide a reference for the development of natural α-glucosidase inhibitors.\",\"PeriodicalId\":12386,\"journal\":{\"name\":\"Foods\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":4.7000,\"publicationDate\":\"2024-09-06\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Foods\",\"FirstCategoryId\":\"97\",\"ListUrlMain\":\"https://doi.org/10.3390/foods13172835\",\"RegionNum\":2,\"RegionCategory\":\"农林科学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q1\",\"JCRName\":\"FOOD SCIENCE & TECHNOLOGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Foods","FirstCategoryId":"97","ListUrlMain":"https://doi.org/10.3390/foods13172835","RegionNum":2,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"FOOD SCIENCE & TECHNOLOGY","Score":null,"Total":0}
引用次数: 0
摘要
α-葡萄糖苷酶是治疗II型糖尿病的一个重要靶点,寻找天然的α-葡萄糖苷酶抑制剂是目前功能食品研究的一个热门话题。山茶苷 A 是 Adinandra nitida 叶子中的主要黄酮类化合物,但有关其抑制α-葡萄糖苷酶的研究却鲜有报道。有鉴于此,本研究系统研究了山茶甙A对α-葡萄糖苷酶的抑制作用,结合荧光法和分子对接法探讨了它们之间的相互作用,旨在揭示相关的抑制机理。结果表明,山茶苷A具有良好的α-葡萄糖苷酶抑制活性(IC50,27.57 ± 0.59 μg/mL),山茶苷A与α-葡萄糖苷酶的结合过程以范德华力和氢键为主,结合位点数为1。分子对接实验表明,山茶苷 A 与α-葡萄糖苷酶的 Glu771、Trp391、Trp710、Gly566、Asp568 和 Phe444 形成氢键结合,与热力学结果一致。我们的研究结果可为天然α-葡萄糖苷酶抑制剂的开发提供参考。
Inhibitory Mechanism of Camellianin A against α-Glucosidase: In Vitro and Molecular Simulation Studies
α-Glucosidase is an important target for type II diabetes treatment, and the search for natural α-glucosidase inhibitors is currently a hot topic in functional food research. Camellianin A is the main flavonoid in the leaves of Adinandra nitida, but research on its inhibition of α-glucosidase is rarely reported. In view of this, the present study systematically investigated the inhibitory impact of camellianin A on α-glucosidase, combining the fluorescence method and molecular docking to explore their interaction, aiming to reveal the relevant inhibitory mechanism. The results indicated that camellianin A possessed excellent α-glucosidase inhibitory activity (IC50, 27.57 ± 0.59 μg/mL), and van der Waals force and hydrogen bonding dominated the binding process between camellianin A and α-glucosidase, with a binding-site number of 1. A molecular docking experiment suggested that camellianin A formed hydrogen bonding with Glu771, Trp391, Trp710, Gly566, Asp568, and Phe444 of α-glucosidase, consistent with the thermodynamic result. Our result can provide a reference for the development of natural α-glucosidase inhibitors.
期刊介绍:
Foods (ISSN 2304-8158) is an international, peer-reviewed scientific open access journal which provides an advanced forum for studies related to all aspects of food research. It publishes reviews, regular research papers and short communications. Our aim is to encourage scientists, researchers, and other food professionals to publish their experimental and theoretical results in as much detail as possible or share their knowledge with as much readers unlimitedly as possible. There is no restriction on the length of the papers. The full experimental details must be provided so that the results can be reproduced. There are, in addition, unique features of this journal:
manuscripts regarding research proposals and research ideas will be particularly welcomed
electronic files or software regarding the full details of the calculation and experimental procedure, if unable to be published in a normal way, can be deposited as supplementary material
we also accept manuscripts communicating to a broader audience with regard to research projects financed with public funds