Binding properties of drospirenone with human serum albumin and lysozyme in vitro.
Binding properties of drospirenone with human serum albumin and lysozyme in vitro.
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DOI：
10.1016/j.saa.2015.09.017
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发表时间：
2016-01
期刊：
影响因子：
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通讯作者：
Qing Wang;Xiangling Ma;Jiawei He;Qiaomei Sun;Yuanzhi Li;Hui Li
中科院分区：
文献类型：
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作者：
Qing Wang;Xiangling Ma;Jiawei He;Qiaomei Sun;Yuanzhi Li;Hui Li
采用不同的光学技术和分子模型研究了屈螺酮（DP）与人血清白蛋白（HSA）/溶菌酶（LYZ）的相互作用。从发射光谱和时间分辨荧光研究结果表明，HSA/LYZ发射猝灭DP引发的静态猝灭机制。LYZ-DP体系比HSA-DP体系更易受温度的影响。置换实验表明，DP结合位点主要位于HSA的位点1。基于对接方法，DP主要结合在Trp-62和Trp-63所在的活性位点铰链区。构象研究表明，DP对HSA和LYZ分子的局部构象有不同的影响。
The interaction of drospirenone (DP) with human serum albumin (HSA)/lysozyme (LYZ) was investigated using different optical techniques and molecular models. Results from the emission and time resolved fluorescence studies revealed that HSA/LYZ emission quenching with DP was initiated by static quenching mechanism. The LYZ–DP system was more easily influenced by temperature than the HSA–DP system. Displacement experiments demonstrated that the DP binding site was mainly located in site 1 of HSA. Based on the docking methods, DP was mainly bound in the active site hinge region where Trp-62 and Trp-63 are located. Conformation study showed that DP had different effects on the local conformation of HSA and LYZ molecules.