title: Kinetic and thermodynamic study of bovine serum albumin interaction with rifampicin using surface plasmon resonance and molecular docking methods.
abstract: The interaction of bovine serum albumin (BSA) with various drugs, such as antibiotics, due to the importance of BSA in drug delivery has attracted increasing research attention at present. Therefore, the aim of this study was investigation of BSA interaction with rifampicin using surface plasmon resonance (SPR) and molecular docking methods under the imitated physiological conditions ( pH = 7.4 ). BSA immobilization on carboxymethyl dextran hydrogel chip has been carried out after activation with N-hydroxysuccinimide/N-ethyl-N-(3-diethylaminopropyl) carbodiimide. The dose-response sensorgrams of BSA upon increasing concentration of refampicin were attained in SPR analysis. The high affinity of rifampicin to BSA was demonstrated by a low equilibrium constants ( K D ) value ( 3.46 × 10 ? 5 at 40°C). The process of kinetic values changing shows that affinity of BSA to rifampicin decreased with rising temperature. The positive value of both enthalpy change ( ? H ) and entropy change ( ? S ) showed that hydrophobic force plays major role in the BSA interaction with rifampicin. The positive value of ? G was indicative of nonspontaneous and enthalpy-driven binding process. In addition, according to the molecular docking study, hydrogen binding has some contributions in the interaction of rifampicin with BSA.
authors.affiliation: University of Tabriz, Research Institute for Applied Physics and Astronomy, Tabriz, Iran.
authors.forename: Maryam
authors.initials: M
authors.lastname: Sharifi
authors.affiliation: Tabriz University of Medical Sciences, Research Center for Pharmaceutical Nanotechnology, Faculty of Pharmacy, Tabriz, Iran.
authors.forename: Jafar Ezzati Nazhad
authors.initials: JE
authors.lastname: Dolatabadi
authors.affiliation: Tabriz University of Medical Sciences, Research Center for Pharmaceutical Nanotechnology, Faculty of Pharmacy, Tabriz, IrancTabriz University of Medical Sciences, Student Research Committee, Tabriz, Iran.
authors.forename: Farzaneh
authors.initials: F
authors.lastname: Fathi
authors.affiliation: Tabriz University of Medical Sciences, Research Center for Pharmaceutical Nanotechnology, Faculty of Pharmacy, Tabriz, Iran.
authors.forename: Mohammad
authors.initials: M
authors.lastname: Rashidi
authors.affiliation: Tabriz University of Medical Sciences, Biotechnology Research Center, Tabriz, Iran.
authors.forename: Behzad
authors.initials: B
authors.lastname: Jafari
authors.affiliation: University of Tabriz, Research Institute for Applied Physics and Astronomy, Tabriz, Iran.
authors.forename: Habib
authors.initials: H
authors.lastname: Tajalli
authors.affiliation: Tabriz University of Medical Sciences, Research Center for Pharmaceutical Nanotechnology, Faculty of Pharmacy, Tabriz, Iran.
authors.forename: Mohammad-Reza
authors.initials: MR
authors.lastname: Rashidi
mesh_terms: D002623:Chemistry Techniques, Analytical / Q000379:methods*; D007700:Kinetics; D062105:Molecular Docking Simulation; D011485:Protein Binding; D012293:Rifampin / Q000378:metabolism*; D012710:Serum Albumin, Bovine / Q000378:metabolism*; D013050:Spectrometry, Fluorescence; D020349:Surface Plasmon Resonance; D013816:Thermodynamics
chemical_list: D012710:Serum Albumin, Bovine; D012293:Rifampin