化学
结合常数
牛血清白蛋白
环糊精
猝灭(荧光)
疏水效应
血清白蛋白
结合位点
对接(动物)
生物信息学
分子模型
荧光光谱法
血浆蛋白结合
生物物理学
圆二色性
荧光
立体化学
生物化学
物理
护理部
基因
生物
医学
量子力学
作者
Shumaila Afrin,Yusra Rahman,Mustafa Alhaji Isa,Shahbaz Ahmed,Mohammad Tabish
标识
DOI:10.1080/07391102.2019.1651220
摘要
The binding characteristic of anti-platelet drug dipyridamole has been investigated with a transport protein, serum albumin. A multi-spectroscopic approach has been employed, and the results were well supported by in silico molecular docking and simulation studies. The fluorescence quenching of serum albumin at three different temperatures revealed that the mechanism involved is static and the binding constant of the interaction was found to be of the order of 104 M−1. The reaction was found to be spontaneous and involved hydrophobic interactions. Synchronous, 3D fluorescence and CD spectroscopy indicated a change in conformation of bovine serum albumin (BSA) on interaction with DP. Using site-selective markers, the binding site of DP was found to be in subdomain IB. Molecular docking studies further corroborated these results. Molecular dynamic (MD) simulations showed lower RMSD values on interaction, suggesting the existence of a stable complex between DP and BSA. Furthermore, since β-Cyclodextrin (βCD) is used to improve the solubility of DP in ophthalmic solutions, therefore, the effect of (βCD) on the interaction of BSA and DP was also studied, and it was found that in the presence of βCD, the binding constant for BSA-DP interaction decreased. The present study is an attempt to characterize the transport of DP and to improve its bioavailability, consequently helping in dosage design to achieve optimum therapeutic levels.Communicated by Ramaswamy H. Sarma
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