Studies on Thermodynamics Features of the Interaction between Imidacloprid and Bovine Serum Albumin

✍ Scribed by Cheng-Nong Yan; Ping Mei; Zhong-Jie Guan; Yi Liu

• Publisher: John Wiley and Sons
• Year: 2007
• Tongue: English
• Weight: 116 KB
• Volume: 25
• Category: Article
• ISSN: 0256-7660
• DOI: 10.1002/cjoc.200790202

✦ Synopsis

Abstract

At different temperatures, the interactions between imidacloprid (IMI) and bovine serum albumin (BSA) were investigated with a fluorescence quenching spectrum, a synchronous fluorescence spectrum, a three‐dimensional fluorescence spectrum and an ultraviolet‐visible spectrum. The average values of bonding constants (K~LB~: 3.424×10^4^ L·mol^−1^), thermodynamic parameters (Δ__H__: 5.188 kJ·mol^−1^, Δ__G__^(^:−26.36 kJ·mol^−1^, Δ__S__: 103.9 J·K^−1^·mol^−1^) and the numbers of bonding sites (n: 1.156) could be obtained through Stern‐Volmer, Lineweaver‐Burk and thermodynamic equations. It was shown that the fluorescence of BSA could be quenched for its reactions with IMI to form a certain kind of new compound. The quenching belonged to a static fluorescence quenching, with a non‐radiation energy transfer happening within a single molecule. The thermodynamic parameters agree with Δ__H__>0, Δ__S__>0 and Δ__G__^σ^<0, suggesting that the binding power between IMI and BSA should be mainly a hydrophobic interaction.