Synthesis and interaction studies of benzimidazole derivative with human serum albumin.
作者： Jianming Liu , Yuanyuan Yue , Muwen Liu , Ningfei Zhang , Kelei Zhuo
DOI: 10.1016/J.SAA.2011.07.052
关键词: Iodide 、 Binding site 、 Nuclear chemistry 、 Analytical chemistry 、 Hydrogen bond 、 Fluorescence 、 Chemistry 、 Benzimidazole 、 Human serum albumin 、 Quenching (fluorescence) 、 Protein secondary structure
摘要: Abstract A benzimidazole derivative, 1-(2-picolyl)-3-(2-picolyl) iodide (PPB), was synthesized. Fourier transform infrared spectroscopy (FT-IR), UV–visible, three-dimensional (3D) fluorescence, synchronous fluorescence (SF) and spectroscopic methods were used to determine the PPB binding mode effects of on protein stability secondary structure. Fluorescence results revealed presence static type quenching mechanism in human serum albumin (HSA). The constants between HSA obtained according Scatchard equation. number sites, thermodynamic parameters measured. showed a spontaneous through hydrogen bonds van der Waals forces. In addition, distance Trp 214 estimated via employing Forster's non-radiative energy transfer theory, found be 3.49 nm, which indicated that can bind with high probability. Site marker competitive experiments primarily took place subdomain IIA.
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