Human serum albumin (HSA) is the most abundant protein in the circulatory system; HSA is an abundant plasma protein that binds a wide variety interaction of [Pd (bipy) Glycine] Cl. The complex [Pd (bipy) Glycine] Cl has been synthesized and purified and the spectral characteristics of this complex were determined and a series of titration experiments were designed with respect to titration of complex with HAS solution. These experiments are done at pH=7, 1mM phosphate buffer and at 20, 25, 30, 37 and 40 ºC. The titration spectra were analyzed at each temperature based on binding models of 1:1, 1:2 and 2:1, using SQUAD software .The results represents the formation of 1:1 complex between drug and HSA .All of the thermodynamic parameters such as Δ G , Δ H , Δ S and formation constant (K) were calculated with their uncertainty. These results were interpreted on the basis of molecular viewpoint and represent the endothermic of process. Hence the process is entropy driven; this confirms the rule of hydrophobic interaction in the formation of drug-HSA complex. This evidence is also certified by studying the effect of ionic strength on the UV-Vis spectra of drug-HSA.
Keywords: [Pd (bipy) Glycine] Cl; HAS; Ionic strength; UV-Vis spectra; Drug delivery
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