Interaction Between Levamisole Hydrochloride and?Bovine Serum Albumin and the Influence of?Alcohol: Spectra

详细信息    查看全文

• 作者：Hua Yan ; Songlin Zhao ; Jianguo Yang ; Xiandi Zhu ; Guoliang Dai ; Huading Liang ; Fuyou Pan and Lin Weng
• 关键词：Levamisole hydrochloride ; Bovine serum albumin ; Alcohol ; Fluorescence spectra ; Interaction
• 刊名：Journal of Solution Chemistry
• 出版年：2009
• 出版时间：September, 2009
• 年：2009
• 卷：38
• 期：9
• 页码：1183-1192
• 全文大小：363.8 KB

文摘

The interaction between levamisole hydrochloride (LH) and bovine serum albumin, BSA, has been studied by a spectral method under physiological conditions. For 1:n complexes, the relationship between fluorescence quenching intensity and concentration of the quenchers can be deduced on the basis of the modified Stern–Volmer equation. The binding constants and corresponding thermodynamic parameters ΔH _m, ΔG _m and ΔS _m at different temperatures were calculated. The experimental results demonstrated that the combination reaction of LH and BSA was a static quenching process because a 1:1 complex was formed, and the main dominant binding forces were hydrogen bonding and van der Waals forces. Meanwhile, the polarity of the tyrosine residue (Tyr) or tryptophan residue (Trp) micro-region was not obviously affected by the interaction. Furthermore, the binding constant increase when alcohol was added.