{"title":"紫外-可见法研究(E)-2-苄基苯并亚酮衍生物与血清白蛋白的相互作用及其对拓扑异构酶的抑制作用","authors":"Z. Rozmer, P. Perjési","doi":"10.25082/jpbr.2020.01.003","DOIUrl":null,"url":null,"abstract":"Interaction of some cyclic chalcone analogs, (E)-2-(4-X-benzylidene)-1-benzosuberone derivatives with bovine serum albumin (BSA) and human serum albumin (HSA) has been investigated using UV-Vis spectroscopic methods. Recording the UV-Vis spectra of compounds in the presence of BSA or HSA indicated interaction of the molecules with the hydrophobic binding site(s) of the proteins. Investigated analogs have shown remarkable topo I and topo II inhibitory activity compared to camptothecin and etoposide, respectively, at 40 μM concentration. The observed interactions between the cyclic chalcone analogs and the cellular macromolecules might play a role in the previously detected cytotoxicity against several tumor cell lines.","PeriodicalId":16703,"journal":{"name":"Journal of Pharmaceutical and Biopharmaceutical Research","volume":"10 1","pages":""},"PeriodicalIF":0.0000,"publicationDate":"2020-08-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"2","resultStr":"{\"title\":\"Study on the interaction of some (E)-2-benzylidenebenzosuberone derivatives with serum albumin by UV-Vis method, inhibitory effect on topoisomerase\",\"authors\":\"Z. Rozmer, P. Perjési\",\"doi\":\"10.25082/jpbr.2020.01.003\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"Interaction of some cyclic chalcone analogs, (E)-2-(4-X-benzylidene)-1-benzosuberone derivatives with bovine serum albumin (BSA) and human serum albumin (HSA) has been investigated using UV-Vis spectroscopic methods. Recording the UV-Vis spectra of compounds in the presence of BSA or HSA indicated interaction of the molecules with the hydrophobic binding site(s) of the proteins. Investigated analogs have shown remarkable topo I and topo II inhibitory activity compared to camptothecin and etoposide, respectively, at 40 μM concentration. The observed interactions between the cyclic chalcone analogs and the cellular macromolecules might play a role in the previously detected cytotoxicity against several tumor cell lines.\",\"PeriodicalId\":16703,\"journal\":{\"name\":\"Journal of Pharmaceutical and Biopharmaceutical Research\",\"volume\":\"10 1\",\"pages\":\"\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2020-08-14\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"2\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Journal of Pharmaceutical and Biopharmaceutical Research\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.25082/jpbr.2020.01.003\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of Pharmaceutical and Biopharmaceutical Research","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.25082/jpbr.2020.01.003","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 2
摘要
利用紫外可见光谱法研究了一些环查尔酮类似物(E)-2-(4- x -苄基)-1-苯并亚酮衍生物与牛血清白蛋白(BSA)和人血清白蛋白(HSA)的相互作用。在BSA或HSA存在下记录化合物的UV-Vis光谱,表明分子与蛋白质的疏水结合位点相互作用。与喜树碱和依托泊苷相比,所研究的类似物在40 μM浓度下分别表现出显著的topo I和topo II抑制活性。环状查尔酮类似物与细胞大分子之间的相互作用可能在先前检测到的对几种肿瘤细胞系的细胞毒性中起作用。
Study on the interaction of some (E)-2-benzylidenebenzosuberone derivatives with serum albumin by UV-Vis method, inhibitory effect on topoisomerase
Interaction of some cyclic chalcone analogs, (E)-2-(4-X-benzylidene)-1-benzosuberone derivatives with bovine serum albumin (BSA) and human serum albumin (HSA) has been investigated using UV-Vis spectroscopic methods. Recording the UV-Vis spectra of compounds in the presence of BSA or HSA indicated interaction of the molecules with the hydrophobic binding site(s) of the proteins. Investigated analogs have shown remarkable topo I and topo II inhibitory activity compared to camptothecin and etoposide, respectively, at 40 μM concentration. The observed interactions between the cyclic chalcone analogs and the cellular macromolecules might play a role in the previously detected cytotoxicity against several tumor cell lines.