{"title":"荧光光谱法研究合成食用色素和盐酸环丙沙星与牛血清白蛋白的竞争相互作用","authors":"Bao-Sheng Liu, Chao Yang, Jing Wang, Chunli Xue, Yun-kai Lü","doi":"10.1155/2011/137531","DOIUrl":null,"url":null,"abstract":"The effects of synthetic food colorants like tartrazine (TTZ), sunset yellow (SY), and erythrosine (ETS) on the binding reaction between ciprofloxacin hydrochloride (CPFX) and bovine serum albumin (BSA) were investigated by fluorescence spectroscopy in the aqueous solution of pH = 7.40. Results showed that CPFX caused the fluorescence quenching of BSA through a static quenching procedure and the primary binding site was located at subdomain IIA of BSA (site I). According to the calculated thermodynamic parameters, it confirmed that CPFX bound to BSA by electrostatic interaction. In addition, the colorants affected the formation of BSA-CPFX complex. This resulted in an increase of the free, biological active fraction of CPFX. The binding distance of BSA-CPFX systems was evaluated according to Forster's theory. Results suggested that the binding distance were increased in the presence of synthetic food colorants.","PeriodicalId":17290,"journal":{"name":"Journal of Thermodynamics","volume":"38 1","pages":"1-7"},"PeriodicalIF":0.0000,"publicationDate":"2011-11-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"3","resultStr":"{\"title\":\"Investigation on the Competition Interaction of Synthetic Food Colorants and Ciprofloxacin Hydrochloride with Bovine Serum Albumin by Fluorescence Spectroscopy\",\"authors\":\"Bao-Sheng Liu, Chao Yang, Jing Wang, Chunli Xue, Yun-kai Lü\",\"doi\":\"10.1155/2011/137531\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"The effects of synthetic food colorants like tartrazine (TTZ), sunset yellow (SY), and erythrosine (ETS) on the binding reaction between ciprofloxacin hydrochloride (CPFX) and bovine serum albumin (BSA) were investigated by fluorescence spectroscopy in the aqueous solution of pH = 7.40. Results showed that CPFX caused the fluorescence quenching of BSA through a static quenching procedure and the primary binding site was located at subdomain IIA of BSA (site I). According to the calculated thermodynamic parameters, it confirmed that CPFX bound to BSA by electrostatic interaction. In addition, the colorants affected the formation of BSA-CPFX complex. This resulted in an increase of the free, biological active fraction of CPFX. The binding distance of BSA-CPFX systems was evaluated according to Forster's theory. Results suggested that the binding distance were increased in the presence of synthetic food colorants.\",\"PeriodicalId\":17290,\"journal\":{\"name\":\"Journal of Thermodynamics\",\"volume\":\"38 1\",\"pages\":\"1-7\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2011-11-16\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"3\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Journal of Thermodynamics\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.1155/2011/137531\",\"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 Thermodynamics","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1155/2011/137531","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Investigation on the Competition Interaction of Synthetic Food Colorants and Ciprofloxacin Hydrochloride with Bovine Serum Albumin by Fluorescence Spectroscopy
The effects of synthetic food colorants like tartrazine (TTZ), sunset yellow (SY), and erythrosine (ETS) on the binding reaction between ciprofloxacin hydrochloride (CPFX) and bovine serum albumin (BSA) were investigated by fluorescence spectroscopy in the aqueous solution of pH = 7.40. Results showed that CPFX caused the fluorescence quenching of BSA through a static quenching procedure and the primary binding site was located at subdomain IIA of BSA (site I). According to the calculated thermodynamic parameters, it confirmed that CPFX bound to BSA by electrostatic interaction. In addition, the colorants affected the formation of BSA-CPFX complex. This resulted in an increase of the free, biological active fraction of CPFX. The binding distance of BSA-CPFX systems was evaluated according to Forster's theory. Results suggested that the binding distance were increased in the presence of synthetic food colorants.