STUDY ON THE INTERACTION OF 2-CARBOXYPHENOXATHIIN WITH BOVINE SERUM ALBUMIN AND HUMAN SERUM ALBUMIN BY FLUORESCENCE SPECTROSCOPY AND CIRCULAR DICHROISM

被引：0

作者：

Varlan, Aurica ^{[1
]}

Hillebrand, Mihaela ^{[1
]}

机构：

[1] Univ Bucharest, Fac Chem, Dept Phys Chem, Bucharest 030018, Romania

来源：

REVUE ROUMAINE DE CHIMIE | 2010年 / 55卷 / 01期

关键词：

steady state fluorescence; synchronous fluorescence; circular dichroism; 2-carboxyphenoxathiin; bovine serum albumin human serum albumin; PHENOXATHIIN DERIVATIVES; BINDING; REAGENT; ACID;

D O I：

暂无

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

The interaction between 2-carboxyphenoxathiin and bovine serum albumin (BSA)/human serum albumin (HSA) has been studied by fluorescence spectroscopy and circular dichroism. The binding of 2-carboxyphenoxathiin quenches the BSA and HSA fluorescence. By the fluorescence quenching results, it was found that the binding constant K=3.2*10(5)/1.09*10(5) M-1, and number of binding sites n = 0.95/0.82. The distance, r, between donor (BSA or HSA) and acceptor. (2-carboxyphenoxathiin) was obtained according to the Forster's theory of non-radiatioactive energy transfer. The interaction between 2-carboxyphenoxathiin and BSA/HSA has been verified as consistent with the static quenching procedure and the quenching mechanism is related to the energy transfer. Circular Dichroism results revealed that the binding of 2-carboxyphenoxathiin to BSA/HSA do not induce conformational changes in albumins.

引用

页码：69 / 77

页数：9

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