Elucidation of binding mechanism of hydroxyurea on serum albumins by different spectroscopic studies.

Elucidation of binding mechanism of hydroxyurea on serum albumins by different spectroscopic studies.
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DOI:
10.1186/2193-1801-3-360
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发表时间:
2014
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影响因子:
--
通讯作者:
Nandibewoor ST
Nandibewoor ST
中科院分区:
其他
文献类型:
--
作者:
Naik KM;Kolli DB;Nandibewoor ST

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羟基脲(HU)与血清白蛋白(SAs)的相互作用尚未被研究。但需要在pH为7.4的磷酸盐缓冲液中研究HU与SAs的相互作用。在体外模拟生理条件下,采用荧光、FT-IR、紫外-可见吸收、同步荧光和三维荧光等光谱方法研究了胡与牛血清白蛋白(BSA)和人血清白蛋白(HSA)的结合。Stern-Volmer图表明,HU与SAs的相互作用存在动态猝灭机制。根据双对数回归曲线得到不同温度下的结合位点数n和结合常数K。FT-IR光谱、紫外-可见吸收光谱、同步荧光光谱和三维荧光光谱结果表明,在HU的存在下,sa的构象发生了改变。根据范霍夫方程计算了热力学参数,并对其进行了讨论。研究牛血清白蛋白、HSA与HU的相互作用对制药、生命科学和临床医学具有重要意义。
The interaction of hydroxyurea (HU) with serum albumins (SAs) has not been investigated so far. However, it necessitates the interaction study of HU with SAs in phosphate buffer of pH 7.4. The binding of HU on bovine serum albumin (BSA) and human serum albumin (HSA) was studied in vitro under simulated physiological conditions by spectroscopic methods viz., fluorescence, FT-IR, UV–vis absorption, synchronous fluorescence and three-dimensional fluorescence. The Stern-Volmer plot indicated the presence of dynamic quenching mechanism in the interaction of HU with SAs. The number of binding sites, n and binding constants, K were obtained at various temperatures according to the double logarithm regression curve. The result of FT-IR spectra, UV–vis absorption, synchronous fluorescence and three-dimensional fluorescence spectra showed that the conformation of SAs has been changed in the presence of HU. The thermodynamic parameters were calculated according to van’t Hoff equation and discussed. This kind of study of interaction between BSA and HSA with HU would be useful in pharmaceutical industry, life sciences and clinical medicine.
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