Byadagi Kirthi, Meti Manjunath, Nandibewoor Sharanappa, Chimatadar Shivamurti
P.G. Department of Studies in Chemistry, Karnatak University, Dharwad 580003, India.
J Pharm Anal. 2017 Apr;7(2):103-109. doi: 10.1016/j.jpha.2016.07.004. Epub 2016 Dec 9.
Interaction of procainamide hydrochloride (PAH) with human serum albumin (HSA) is of great significance in understanding the pharmacokinetic and pharmacodynamic mechanisms of the drug. Multi-spectroscopic techniques were used to investigate the binding mode of PAH to HSA and results revealed the presence of static type of quenching mechanism. The number of binding sites, binding constants and thermodynamic parameters were calculated. The results showed a spontaneous binding of PAH to HSA and hydrophobic interactions played a major role. In addition, the distance between PAH and the Trp-214 was estimated employing the Förster's theory. Site marker competitive experiments indicated that the binding of PAH to HSA primarily took place in subdomain IIA (Sudlow's site I). The influence of interference of some common metal ions on the binding of PAH to HSA was studied. Synchronous fluorescence spectra (SFS), 3D fluorescence spectra and circular dichroism (CD) results indicated the conformational changes in the structure of HSA.
盐酸普鲁卡因胺（PAH）与人血清白蛋白（HSA）的相互作用对于理解该药物的药代动力学和药效学机制具有重要意义。采用多种光谱技术研究了PAH与HSA的结合模式，结果表明存在静态猝灭机制。计算了结合位点数量、结合常数和热力学参数。结果表明PAH与HSA的结合是自发的，疏水相互作用起主要作用。此外，利用Förster理论估算了PAH与Trp-214之间的距离。位点标记竞争实验表明，PAH与HSA的结合主要发生在亚结构域IIA（Sudlow位点I）。研究了一些常见金属离子的干扰对PAH与HSA结合的影响。同步荧光光谱（SFS）、三维荧光光谱和圆二色性（CD）结果表明HSA结构发生了构象变化。
