期刊
JOURNAL OF LUMINESCENCE
卷 121, 期 1, 页码 179-186出版社
ELSEVIER
DOI: 10.1016/j.jlumin.2005.12.001
关键词
bovine serum albumin; trazodone hydrochloride; interactions
类别
In this paper, the binding of trazodone hydrochloride (TZH) to bovine serum albumin (BSA) was investigated by spectroscopic (fluorescence, spectrophotometry and circular dichroism) techniques under simulative physiological conditions. A strong fluorescence quenching reaction of TZH to BSA was observed and the quenching mechanism was suggested as dynamic quenching according to the Stern-Volmer equation. The binding constants of TZH with BSA at 288, 302 and 309K were calculated as (1.56 +/- 0.003)x 10(4), (2.31 +/- 0.002) x 10(4) and (5.44 +/- 0.004) x 10(4) M-1, respectively. The thermodynamic parameters, Delta H-0 and Delta S-0 were obtained to be 39.86 +/- 0.008 kJ mol(-1) and 217.89 +/- 0.011 J mol(-1) K-1, respectively, which indicated the presence of hydrophobic forces between TZH and BSA. The spectral results observed showed that the binding of TZH to BSA induced conformational changes in BSA. Based on the Forster's theory of non-radiation energy transfer, the binding average distance, r between donor (BSA) and acceptor (TZH) was found to be 2.4 nm. The effect of common ions on binding of TZH to BSA was also examined. (c) 2005 Elsevier B.V. All rights reserved.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据