{"title":"葛根素对 CYP1B1 酶抑制活性的量子化学分析和生物化学评价","authors":"Xue Li, Jinyue Lu, Lianrong Yang, Yuan Tian, Liwei Jia, Xin Meng","doi":"10.1093/chemle/upae160","DOIUrl":null,"url":null,"abstract":"The inhibitory activity of puerarin on the CYP1B1 enzyme was evaluated by the 7-ethoxyresorufin O-dealkylation method. At the same time, the density functional theory algorithm, molecular docking, and molecular dynamics simulations were used to verify the stability of the puerarin–CYP1B1 complex. It has been found that puerarin is a potent uncompetitive inhibitor of CYP1B1 (IC50: 1.06 ± 0.15 μM).","PeriodicalId":9862,"journal":{"name":"Chemistry Letters","volume":null,"pages":null},"PeriodicalIF":1.4000,"publicationDate":"2024-08-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Quantum chemical analysis and biochemical evaluation of the inhibitory activity of puerarin on CYP1B1 enzyme\",\"authors\":\"Xue Li, Jinyue Lu, Lianrong Yang, Yuan Tian, Liwei Jia, Xin Meng\",\"doi\":\"10.1093/chemle/upae160\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"The inhibitory activity of puerarin on the CYP1B1 enzyme was evaluated by the 7-ethoxyresorufin O-dealkylation method. At the same time, the density functional theory algorithm, molecular docking, and molecular dynamics simulations were used to verify the stability of the puerarin–CYP1B1 complex. It has been found that puerarin is a potent uncompetitive inhibitor of CYP1B1 (IC50: 1.06 ± 0.15 μM).\",\"PeriodicalId\":9862,\"journal\":{\"name\":\"Chemistry Letters\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":1.4000,\"publicationDate\":\"2024-08-24\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Chemistry Letters\",\"FirstCategoryId\":\"92\",\"ListUrlMain\":\"https://doi.org/10.1093/chemle/upae160\",\"RegionNum\":4,\"RegionCategory\":\"化学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q3\",\"JCRName\":\"CHEMISTRY, MULTIDISCIPLINARY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Chemistry Letters","FirstCategoryId":"92","ListUrlMain":"https://doi.org/10.1093/chemle/upae160","RegionNum":4,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q3","JCRName":"CHEMISTRY, MULTIDISCIPLINARY","Score":null,"Total":0}
Quantum chemical analysis and biochemical evaluation of the inhibitory activity of puerarin on CYP1B1 enzyme
The inhibitory activity of puerarin on the CYP1B1 enzyme was evaluated by the 7-ethoxyresorufin O-dealkylation method. At the same time, the density functional theory algorithm, molecular docking, and molecular dynamics simulations were used to verify the stability of the puerarin–CYP1B1 complex. It has been found that puerarin is a potent uncompetitive inhibitor of CYP1B1 (IC50: 1.06 ± 0.15 μM).