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

Abstract

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.

Resveratrol reduced the detrimental effects of malondialdehyde on human endothelial cells

“…SPR method was used to measure the interaction of Res and MDA with the serum albumin (BSA). 23 , 24 Trace DrawerTM for SPR NaviTM was applied for calculations of affinity and kinetics of the measured interaction. At pH 7.4 the affinity unit (K D ) for RES and MDA were 2.25 × 10 -4 M and 3.05 × 10 -4 M, respectively ( Figure 4A ).…”

Exploring The Interactions of a Natural Gamma-Oryzanol with Human Serum Albumin: Surface Plasmon Resonance, Fluorescence, and Molecular Modeling Studies

“…To investigate the interaction of ORY with immobilized HSA, various concentrations of ORY were injected into the chip surface and, then, the SPR signals were recorded. Using SPR data analysis, kinetic parameters including K a (association rate constant; the number of HSA-ORY complex formed per second), K d (dissociation rate constant; the decayed fraction of HSA-ORY complex per second) and [33]. SPR, a real-time and label-free method, is one of the most important optical biosensing technologies which is widely used in different areas such as biochemistry, biology, and medical sciences.…”

Personalized Medicine for Antibiotics: The Role of Nanobiosensors in Therapeutic Drug Monitoring

“…This light generates the excitation of a surface plasmon for a certain angle of incidence of said light, known as the resonance angle. The binding of the analytes with their recognition element induces a change in the refractive index and as a consequence the displacement of the resonance angle [ 275 , 293 ]. This type of biosensor has been used in different applications, such as in the clinic where tobramycin has been detected in patient serum based on a portable, palm-sized localized surface transmission plasmon resonance (T-LSPR) configuration.…”