磷霉素与牛血清白蛋白结合相互作用的多光谱研究
Multi-spectroscopic investigation of the binding interaction of fosfomycin with bovine serum albumin.
作者信息
Meti Manjunath D, Nandibewoor Sharanappa T, Joshi Shrinivas D, More Uttam A, Chimatadar Shivamurti A
机构信息
Post Graduate Department of Studies in Chemistry, Karnatak University, Pavate Nagar, Dharwad 580003, Karnataka, India.
Novel Drug Design and Discovery Laboratory, Department of Pharmaceutical Chemistry, S.E.T's College of Pharmacy, Sangolli Rayanna Nagar, Dharwad 580002, Karnataka, India.
出版信息
J Pharm Anal. 2015 Aug;5(4):249-255. doi: 10.1016/j.jpha.2015.01.004. Epub 2015 Feb 14.
The interaction between fosfomycin (FOS) and bovine serum albumin (BSA) has been investigated effectively by multi-spectroscopic techniques under physiological pH 7.4. FOS quenched the intrinsic fluorescence of BSA via static quenching. The number of binding sites and observed binding constant were measured by the fluorescence quenching method. The thermodynamic parameters Δ, Δ and Δ were calculated at different temperatures according to the van't Hoff equation. The site of binding of FOS in the protein was proposed to be Sudlow's site I based on displacement experiments using site markers viz. warfarin, ibuprofen and digitoxin. The distance between the donor (BSA) and acceptor (FOS) molecules was obtained according to the Förster theory. The effect of FOS on the conformation of BSA was analyzed using synchronous fluorescence spectra (SFS), circular dichroism (CD) and 3D fluorescence spectra. A molecular modeling study further confirmed the binding mode obtained by the experimental studies.
在生理pH值7.4条件下，采用多种光谱技术对磷霉素（FOS）与牛血清白蛋白（BSA）之间的相互作用进行了有效研究。FOS通过静态猝灭作用猝灭了BSA的固有荧光。采用荧光猝灭法测定了结合位点数量和观察到的结合常数。根据范特霍夫方程，在不同温度下计算了热力学参数ΔH、ΔS和ΔG。基于使用位点标记物华法林、布洛芬和地高辛的置换实验，推测FOS在蛋白质中的结合位点为Sudlow位点I。根据Förster理论获得了供体（BSA）和受体（FOS）分子之间的距离。利用同步荧光光谱（SFS）、圆二色性（CD）和三维荧光光谱分析了FOS对BSA构象的影响。分子模拟研究进一步证实了实验研究获得的结合模式。
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