Spectroscopic investigations on the binding of Pyronin Y to human serum albumin
Spectroscopic investigations on the binding of Pyronin Y to human serum albumin
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DOI：
10.1080/07391102.2015.1128357
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发表时间：
2017-01
影响因子：
4.4
通讯作者：
A. Salcı;M. Toprak
中科院分区：
文献类型：
--
作者：
A. Salcı;M. Toprak
采用荧光光谱、吸收光谱、荧光衰减寿命、红外光谱、同步荧光光谱和分子模拟等方法系统研究了派洛宁Y与人血清白蛋白（HSA）的相互作用。光谱和荧光猝灭实验表明，派洛宁Y对HSA的猝灭机制可能是静态的。用Förster非辐射能量转移法测得焦宁Y与人血清白蛋白的特异性结合距离为1.96 nm。热力学参数表明，静电相互作用在结合过程中起着重要的作用。同步荧光光谱和红外光谱分析表明，焦宁Y的加入对HSA的构象和微环境没有影响。所得结果在光动力学治疗中具有生物学意义。
The interaction of Pyronin Y with human serum albumin (HSA) has been investigated systematically by fluorescence, absorption, fluorescence decay lifetime measurements, FTIR, synchronous fluorescence spectroscopy, and molecular modeling method. The spectroscopic and fluorescence quenching experiments show that Pyronin Y may show a static quenching mechanism with HSA. The specific binding distance of 1.96 nm between HSA and Pyronin Y was obtained via Förster non-radiation energy transfer method. The thermodynamic parameters indicate that the electrostatic interactions play a significant role during the binding process. In addition, synchronous fluorescence and FT-IR spectra indicated that the conformation and microenvironment of HSA were not influenced with the addition of Pyronin Y. The obtained results can be of biological significance in photodynamic therapy.