title: Synthesis and interaction studies of benzimidazole derivative with human serum albumin.
abstract: A benzimidazole derivative, 1-(2-picolyl)-3-(2-picolyl) benzimidazole iodide (PPB), was synthesized. Fourier transform infrared spectroscopy (FT-IR), UV-visible, three-dimensional (3D) fluorescence, synchronous fluorescence (SF) and fluorescence spectroscopic methods were used to determine the PPB binding mode and the effects of PPB on protein stability and secondary structure. Fluorescence results revealed the presence of static type of quenching mechanism in the binding of PPB to human serum albumin (HSA). The binding constants between PPB and HSA were obtained according to Scatchard equation. The number of binding sites, the binding constants and the thermodynamic parameters were measured. The results showed a spontaneous binding of PPB to HSA through hydrogen bonds and van der Waals forces. In addition, the distance between PPB and the Trp 214 was estimated via employing the Förster's non-radiative energy transfer theory, and was found to be 3.49 nm, which indicated that PPB can bind to HSA with high probability. Site marker competitive experiments indicated that the binding of PPB to HSA primarily took place in subdomain IIA.
authors.affiliation: School of Chemistry and Environmental Science, Henan Normal University, Xinxiang, Henan 453007, PR China.
authors.forename: Jianming
authors.initials: J
authors.lastname: Liu
authors.forename: Yuanyuan
authors.initials: Y
authors.lastname: Yue
authors.forename: Muwen
authors.initials: M
authors.lastname: Liu
authors.forename: Ningfei
authors.initials: N
authors.lastname: Zhang
authors.forename: Kelei
authors.initials: K
authors.lastname: Zhuo
mesh_terms: D001562:Benzimidazoles / Q000737:chemistry*; D001665:Binding Sites; D002626:Chemistry, Pharmaceutical / Q000379:methods; D015195:Drug Design; D006801:Humans; D006860:Hydrogen Bonding; D007700:Kinetics; D011485:Protein Binding; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D012709:Serum Albumin / Q000737:chemistry*; D013056:Spectrophotometry, Ultraviolet / Q000379:methods; D017550:Spectroscopy, Fourier Transform Infrared / Q000379:methods; D013816:Thermodynamics; D014364:Tryptophan / Q000737:chemistry
chemical_list: D001562:Benzimidazoles; D012709:Serum Albumin; D014364:Tryptophan