Spectroscopic and molecular modeling of the binding of meso-tetrakis(4-hydroxyphenyl)porphyrin to human serum albumin
Spectroscopic and molecular modeling of the binding of meso-tetrakis(4-hydroxyphenyl)porphyrin to human serum albumin
复制标题
内消旋四（4-羟基苯基）卟啉与人血清白蛋白结合的光谱和分子模型
DOI：
10.1016/j.dyepig.2008.08.004
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发表时间：
2009-04-01
影响因子：
4.5
通讯作者：
Shuang, Shaomin
中科院分区：
文献类型：
--
作者：
An, Wenting;Jiao, Yong;Shuang, Shaomin
用荧光光谱、紫外-可见吸收光谱、傅里叶变换红外光谱、圆二色光谱和分子模拟相结合的方法研究了Meso-四(4-羟基苯基)卟啉与人血清白蛋白的结合。荧光和UV-Vis数据表明，疏水相互作用是结合的主要驱动力，着色剂的聚集对染料与血清的亲和力起主要作用。根据Forster非辐射能量转移理论确定染料-血清距离r接近于4 nm。FT-IR和CD光谱分析表明，结合诱导了血清的构象变化，从而降低了蛋白质的x-螺旋结构。分子模拟表明，着色剂可以通过疏水和氢键作用部分插入到IIIA亚区的II位。(C)2008爱思唯尔有限公司。保留所有权利。
The binding of meso-tetrakis(4-hydroxyphenyl)porphyrin to human serum albumin has been investigated by the combination of fluorescence, UV-vis absorption, Fourier transform infrared, circular dichroism spectroscopies and molecular modeling. Fluorescence and UV-vis data indicated that hydrophobic interaction is the main driving force for binding and that aggregation of the colorant plays a major role in the affinity of the dye for the serum. The dye-serum distance, r, was determined to be similar to 4 nm based on Forster non-radiative energy transfer theory. FT-IR and CD spectral examinations revealed that binding induces a conformational change in the serum which reduces the x-helix structure of the protein. Molecular modeling suggested that the colorant can partially insert into the site II of subdomain IIIA via hydrophobic and hydrogen bonding interactions. (C) 2008 Elsevier Ltd. All rights reserved.