Surface plasmon resonance and molecular docking studies of bovine serum albumin interaction with neomycin: kinetic and thermodynamic analysis

Introduction: The interactions between biomacromolecules such as serum albumin (SA) and various drugs have attracted increasing research attention in recent years. However, the study of SA with those drugs that have relatively high hydrophilicity and a lower affinity for SA could be a challenging issue. At the present study, the interaction of bovine SA (BSA) with neomycin as a hydrophilic drug has been investigated using surface plasmon resonance (SPR) and molecular docking methods.

Methods: BSA was immobilized on the carboxymethyl dextran hydrogel sensor chip after activation of carboxylic groups through NHS/EDC and, then, the neomycin interaction with BSA at different concentrations (1-128 µM) was investigated.

Results: Dose-response sensorgrams of BSA upon increasing concentration of neomycin has been shown through SPR analysis. The small KD value (4.96 e-7 at 40°C) demonstrated high affinity of neomycin to BSA. Thermodynamic parameters were calculated through van’t Hoff equation at 4 different temperatures. The results showed that neomycin interacts with BSA via Van der Waals interactions and hydrogen bonds and increase of KD with temperature rising indicated that the binding process was entropy driven. Molecular docking study confirmed that hydrogen bond was the major intermolecular force stabilizing neomycin-BSA complex.

Conclusion: The attained results showed that neomycin molecules can efficiently distribute within the body after interaction with BSA in spite of having hydrophilic properties. Besides, SPR can be considered as a useful instrument for study of the interaction of hydrophilic drugs with SA.

Publication year: 2017
Authors: Sharifi M. 1, Dolatabadi J.E.N. 2, Fathi F. 2,3, Zakariazadeh M. 4, Barzegar A. 4, Rashidi M. 2, Tajalli H. 1, Rashidi M.-R. 2
1 – Research Institute for Applied Physics and Astronomy, University of Tabriz, Tabriz, Iran
2 – Research Center for Pharmaceutical Nanotechnology, Faculty of Pharmacy, Tabriz University of Medical Sciences, Tabriz, Iran
3 – Student Research Committee, Tabriz University of Medical Sciences, Tabriz, Iran
4 – Research Institute for Fundamental Sciences (RIFS), University of Tabriz, Tabriz, Iran
Published in: BioImpacts, 2017, Vol. 7(2), p. 91–97
DOI: 10.15171/bi.2017.12


antibiotic binding affinity CMD sensor slides drug-protein interaction entalphy entropy hydrophilic drug kinetics measured in different temperatures molecular modelling protein (BSA) small molecular weight drug (neomycin) thermodynamic study


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