title: Probing the behavior of bovine serum albumin upon binding to atenolol: insights from spectroscopic and molecular docking approaches.
abstract: Molecular interaction of atenolol, a selective β1receptor antagonist with the major carrier protein, bovine serum albumin (BSA), was investigated under imitated physiological conditions (pH 7.4) by means of fluorescence spectroscopy, UV absorption spectroscopy, Fourier transform infrared spectroscopy (FT-IR), and molecular modeling studies. The steady-state fluorescence spectra manifested that static type, due to formation of the atenolol-BSA complex, was the dominant mechanism for fluorescence quenching. The characteristic information about the binding interaction of atenolol with BSA in terms of binding constant (Kb) were determined by the UV-vis absorption titration, and were found to be in the order of 103M-1at different temperatures, indicating the existence of a weak binding in this system. Thermodynamic analysis revealed that the binding process was primarily mediated by van der Waals force and hydrogen bonds due to the negative sign for enthalpy change (ΔH0), entropy change (ΔS0). The molecular docking results elucidated that atenolol preferred binding on the site II of BSA according to the findings observed in competitive binding experiments. Moreover, via alterations in synchronous fluorescence, three-dimensional fluorescence and FT-IR spectral properties, it was concluded that atenolol could arouse slight configurational and micro-environmental changes of BSA.
authors.affiliation: a College of Pharmaceutical Science , Zhejiang University of Technology , Hangzhou , China.
authors.forename: Tuo-Ying
authors.initials: TY
authors.lastname: Jiang
authors.affiliation: a College of Pharmaceutical Science , Zhejiang University of Technology , Hangzhou , China.
authors.forename: Kai-Li
authors.initials: KL
authors.lastname: Zhou
authors.affiliation: a College of Pharmaceutical Science , Zhejiang University of Technology , Hangzhou , China.
authors.forename: Yan-Yue
authors.initials: YY
authors.lastname: Lou
authors.affiliation: a College of Pharmaceutical Science , Zhejiang University of Technology , Hangzhou , China.
authors.forename: Dong-Qi
authors.initials: DQ
authors.lastname: Pan
authors.affiliation: a College of Pharmaceutical Science , Zhejiang University of Technology , Hangzhou , China.
authors.forename: Jie-Hua
authors.identifier: http://orcid.org/0000-0002-9807-5654
authors.initials: JH
authors.lastname: Shi
mesh_terms: D000818:Animals; D001262:Atenolol / Q000737:chemistry* / Q000378:metabolism; D001665:Binding Sites; D002417:Cattle; D006860:Hydrogen Bonding; D008968:Molecular Conformation; D062105:Molecular Docking Simulation; D056004:Molecular Dynamics Simulation; D015394:Molecular Structure; D011485:Protein Binding; D012710:Serum Albumin, Bovine / Q000737:chemistry* / Q000378:metabolism; D013050:Spectrometry, Fluorescence; D013056:Spectrophotometry, Ultraviolet; D017550:Spectroscopy, Fourier Transform Infrared; D013057:Spectrum Analysis; D013329:Structure-Activity Relationship; D013816:Thermodynamics
chemical_list: D012710:Serum Albumin, Bovine; D001262:Atenolol
keywords: atenolol; bovine serum albumin; interaction; molecular docking; spectroscopy