Research Papers: Sensing

Kinetic and thermodynamic study of bovine serum albumin interaction with rifampicin using surface plasmon resonance and molecular docking methods

[+] Author Affiliations
Maryam Sharifi, Habib Tajalli

University of Tabriz, Research Institute for Applied Physics and Astronomy, Tabriz, Iran

Jafar Ezzati Nazhad Dolatabadi, Mohammad Rashidi, Mohammad-Reza Rashidi

Tabriz University of Medical Sciences, Research Center for Pharmaceutical Nanotechnology, Faculty of Pharmacy, Tabriz, Iran

Farzaneh Fathi

Tabriz University of Medical Sciences, Research Center for Pharmaceutical Nanotechnology, Faculty of Pharmacy, Tabriz, Iran

Tabriz University of Medical Sciences, Student Research Committee, Tabriz, Iran

Behzad Jafari

Tabriz University of Medical Sciences, Biotechnology Research Center, Tabriz, Iran

J. Biomed. Opt. 22(3), 037002 (Mar 02, 2017). doi:10.1117/1.JBO.22.3.037002
History: Received November 15, 2016; Accepted February 10, 2017
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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 (KD) value (3.46×105 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 (ΔH) and entropy change (ΔS) showed that hydrophobic force plays major role in the BSA interaction with rifampicin. The positive value of ΔG 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.

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© 2017 Society of Photo-Optical Instrumentation Engineers

Citation

Maryam Sharifi ; Jafar Ezzati Nazhad Dolatabadi ; Farzaneh Fathi ; Mohammad Rashidi ; Behzad Jafari, et al.
"Kinetic and thermodynamic study of bovine serum albumin interaction with rifampicin using surface plasmon resonance and molecular docking methods", J. Biomed. Opt. 22(3), 037002 (Mar 02, 2017). ; http://dx.doi.org/10.1117/1.JBO.22.3.037002


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