P. Nguyen, N. Trịnh, Thi-Thuy Do, T. Vu, D. To, Hong Khuyen Thi Pham, Phu Chi Hieu Truong, Kim Thuong Pham Van, Manh Hung Tran
{"title":"变叶赤松中潜在的蛋白酪氨酸磷酸酶 1B 和α-葡萄糖苷酶抑制黄酮类化合物:实验和计算结果","authors":"P. Nguyen, N. Trịnh, Thi-Thuy Do, T. Vu, D. To, Hong Khuyen Thi Pham, Phu Chi Hieu Truong, Kim Thuong Pham Van, Manh Hung Tran","doi":"10.1177/17475198231226382","DOIUrl":null,"url":null,"abstract":"Erythrina variegata L., a member of the Fabaceae family, is a valuable medicinal plant with a rich history of traditional medicinal uses. However, its potential as an antidiabetic agent has remained largely unexplored. In this study, three isoflavonoid compounds, namely eryvarin M (1), eryvarin H (2), and neobavaisoflavone (3), were isolated from E. variegata. These compounds displayed significant inhibitory effects on both protein tyrosine phosphatase 1B and α-glucosidase enzymes. The specific attachment position of the prenyl group to the isoflavonoid skeleton plays a pivotal role in determining the variation in their activity. Moreover, the results obtained from docking simulations corroborate the experimental findings, confirming the robust binding affinities of these metabolites toward the target proteins. The docking analysis further highlights that these compounds exhibit highly negative values of binding-free energies against proteins, indicative of their favorable binding affinities. In addition, the formation of hydrogen bonds in the binding region contributes to their binding interactions. These findings significantly enhance our understanding of the therapeutic potential of both E. variegata and its isoflavonoids as potential inhibitors for diabetes and related metabolic disorders, shedding light on their promising role in the field of diabetes research.","PeriodicalId":1,"journal":{"name":"Accounts of Chemical Research","volume":"165 5","pages":""},"PeriodicalIF":16.4000,"publicationDate":"2024-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Potential protein tyrosine phosphatase 1B and α-glucosidase inhibitory flavonoids from Erythrina variegata: Experimental and computational results\",\"authors\":\"P. Nguyen, N. Trịnh, Thi-Thuy Do, T. Vu, D. To, Hong Khuyen Thi Pham, Phu Chi Hieu Truong, Kim Thuong Pham Van, Manh Hung Tran\",\"doi\":\"10.1177/17475198231226382\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"Erythrina variegata L., a member of the Fabaceae family, is a valuable medicinal plant with a rich history of traditional medicinal uses. However, its potential as an antidiabetic agent has remained largely unexplored. In this study, three isoflavonoid compounds, namely eryvarin M (1), eryvarin H (2), and neobavaisoflavone (3), were isolated from E. variegata. These compounds displayed significant inhibitory effects on both protein tyrosine phosphatase 1B and α-glucosidase enzymes. The specific attachment position of the prenyl group to the isoflavonoid skeleton plays a pivotal role in determining the variation in their activity. Moreover, the results obtained from docking simulations corroborate the experimental findings, confirming the robust binding affinities of these metabolites toward the target proteins. The docking analysis further highlights that these compounds exhibit highly negative values of binding-free energies against proteins, indicative of their favorable binding affinities. In addition, the formation of hydrogen bonds in the binding region contributes to their binding interactions. These findings significantly enhance our understanding of the therapeutic potential of both E. variegata and its isoflavonoids as potential inhibitors for diabetes and related metabolic disorders, shedding light on their promising role in the field of diabetes research.\",\"PeriodicalId\":1,\"journal\":{\"name\":\"Accounts of Chemical Research\",\"volume\":\"165 5\",\"pages\":\"\"},\"PeriodicalIF\":16.4000,\"publicationDate\":\"2024-01-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Accounts of Chemical Research\",\"FirstCategoryId\":\"92\",\"ListUrlMain\":\"https://doi.org/10.1177/17475198231226382\",\"RegionNum\":1,\"RegionCategory\":\"化学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q1\",\"JCRName\":\"CHEMISTRY, MULTIDISCIPLINARY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Accounts of Chemical Research","FirstCategoryId":"92","ListUrlMain":"https://doi.org/10.1177/17475198231226382","RegionNum":1,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"CHEMISTRY, MULTIDISCIPLINARY","Score":null,"Total":0}
Potential protein tyrosine phosphatase 1B and α-glucosidase inhibitory flavonoids from Erythrina variegata: Experimental and computational results
Erythrina variegata L., a member of the Fabaceae family, is a valuable medicinal plant with a rich history of traditional medicinal uses. However, its potential as an antidiabetic agent has remained largely unexplored. In this study, three isoflavonoid compounds, namely eryvarin M (1), eryvarin H (2), and neobavaisoflavone (3), were isolated from E. variegata. These compounds displayed significant inhibitory effects on both protein tyrosine phosphatase 1B and α-glucosidase enzymes. The specific attachment position of the prenyl group to the isoflavonoid skeleton plays a pivotal role in determining the variation in their activity. Moreover, the results obtained from docking simulations corroborate the experimental findings, confirming the robust binding affinities of these metabolites toward the target proteins. The docking analysis further highlights that these compounds exhibit highly negative values of binding-free energies against proteins, indicative of their favorable binding affinities. In addition, the formation of hydrogen bonds in the binding region contributes to their binding interactions. These findings significantly enhance our understanding of the therapeutic potential of both E. variegata and its isoflavonoids as potential inhibitors for diabetes and related metabolic disorders, shedding light on their promising role in the field of diabetes research.
期刊介绍:
Accounts of Chemical Research presents short, concise and critical articles offering easy-to-read overviews of basic research and applications in all areas of chemistry and biochemistry. These short reviews focus on research from the author’s own laboratory and are designed to teach the reader about a research project. In addition, Accounts of Chemical Research publishes commentaries that give an informed opinion on a current research problem. Special Issues online are devoted to a single topic of unusual activity and significance.
Accounts of Chemical Research replaces the traditional article abstract with an article "Conspectus." These entries synopsize the research affording the reader a closer look at the content and significance of an article. Through this provision of a more detailed description of the article contents, the Conspectus enhances the article's discoverability by search engines and the exposure for the research.