Bo Zhou , Zu-De Qi , Qi Xiao , Jia-Xin Dong , Ye-Zhong Zhang , Yi Liu
{"title":"荧光猝灭法研究氯雷他定与血清白蛋白的相互作用","authors":"Bo Zhou , Zu-De Qi , Qi Xiao , Jia-Xin Dong , Ye-Zhong Zhang , Yi Liu","doi":"10.1016/j.jbbm.2007.04.001","DOIUrl":null,"url":null,"abstract":"<div><p>The interactions between loratadine and bovine serum albumin (BSA) and human serum albumin (HSA) were studied using tryptophan fluorescence quenching method. The fluorescence intensity of the two serum albumins could be quenched 70% at the molar ratio [loratadine]:[BSA (or HSA)]<!--> <!-->=<!--> <!-->10:1. In the linear range (0–50 μmol L<sup>−<!--> <!-->1</sup>) quenching constants were calculated using Stern–Volmer equation. Temperature in the range 298 K–310 K had a significant effect (<em>p</em> <!--><<!--> <!-->0.05) on the two serum albumins through ANOVA analysis and <em>t</em>-test. Furthermore the conformation changes in the interactions were studied using FTIR spectroscopy.</p></div>","PeriodicalId":15257,"journal":{"name":"Journal of biochemical and biophysical methods","volume":null,"pages":null},"PeriodicalIF":0.0000,"publicationDate":"2007-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.jbbm.2007.04.001","citationCount":"74","resultStr":"{\"title\":\"Interaction of loratadine with serum albumins studied by fluorescence quenching method\",\"authors\":\"Bo Zhou , Zu-De Qi , Qi Xiao , Jia-Xin Dong , Ye-Zhong Zhang , Yi Liu\",\"doi\":\"10.1016/j.jbbm.2007.04.001\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>The interactions between loratadine and bovine serum albumin (BSA) and human serum albumin (HSA) were studied using tryptophan fluorescence quenching method. The fluorescence intensity of the two serum albumins could be quenched 70% at the molar ratio [loratadine]:[BSA (or HSA)]<!--> <!-->=<!--> <!-->10:1. In the linear range (0–50 μmol L<sup>−<!--> <!-->1</sup>) quenching constants were calculated using Stern–Volmer equation. Temperature in the range 298 K–310 K had a significant effect (<em>p</em> <!--><<!--> <!-->0.05) on the two serum albumins through ANOVA analysis and <em>t</em>-test. Furthermore the conformation changes in the interactions were studied using FTIR spectroscopy.</p></div>\",\"PeriodicalId\":15257,\"journal\":{\"name\":\"Journal of biochemical and biophysical methods\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2007-08-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1016/j.jbbm.2007.04.001\",\"citationCount\":\"74\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Journal of biochemical and biophysical methods\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/S0165022X07000814\",\"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 biochemical and biophysical methods","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S0165022X07000814","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Interaction of loratadine with serum albumins studied by fluorescence quenching method
The interactions between loratadine and bovine serum albumin (BSA) and human serum albumin (HSA) were studied using tryptophan fluorescence quenching method. The fluorescence intensity of the two serum albumins could be quenched 70% at the molar ratio [loratadine]:[BSA (or HSA)] = 10:1. In the linear range (0–50 μmol L− 1) quenching constants were calculated using Stern–Volmer equation. Temperature in the range 298 K–310 K had a significant effect (p < 0.05) on the two serum albumins through ANOVA analysis and t-test. Furthermore the conformation changes in the interactions were studied using FTIR spectroscopy.
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