Kinetic studies of bovine serum albumin interaction with PG and TBHQ using surface plasmon resonance

Fathi, Farzaneh; Dolatanbadi, Jafar Ezzati Nazhad; Rashidi, Mohammad-Reza; Omidi, Yadollah

doi:10.1016/j.ijbiomac.2016.06.054

Cited by 41 publications

(23 citation statements)

References 40 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Overall, the results of kinetic study showed that interaction of BSA with neomycin increases upon rising temperature. 6,30 …”

Section: Discussionmentioning

confidence: 99%

“…3-5 Bovine SA (BSA) is the most frequently used protein in the drug-protein interaction studies due to its structural homology with human SA (HSA), cheapness, easy availability and considerable stability. 6,7 It is a large monomeric protein (66 kDa) consisting of about 583 amino acid residues as single chain. The chain is made up of three homologous but structurally distinct domains (I-III); each consisting of 2 subdomains (A and B).…”

Section: Introductionmentioning

confidence: 99%

“…Surface plasmon pesonance (SPR) is a surface-sensitive label-free technique that offers voluble information about molecular interactions, 13,14 characterizing binding reactions, 6 measuring reaction kinetics, 15-17 thermodynamic parameters, 16 affinity constants, 18 etc with high sensitivity. Owing to these properties and abilities, SPR technology has rapidly become a standard tool within the pharmaceutical and biotechnology industries.…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

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

Sharifi¹,

Dolatabadi²,

Fathi³

et al. 2017

Bioimpacts

Self Cite

View full text Add to dashboard Cite

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.

show abstract

“…Overall, the results of kinetic study showed that interaction of BSA with neomycin increases upon rising temperature. 6,30 …”

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

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

Sharifi¹,

Dolatabadi²,

Fathi³

et al. 2017

Bioimpacts

Self Cite

View full text Add to dashboard Cite

show abstract

“…14 For this purpose, a bare Au slide was immersed in a solution containing MUA and Milli-Q-water in a ratio of 7:3. The slide was incubated at room temperature (~25°C) for 20 h and washed thrice with ethanol and then rinsed with phosphate buffered saline (PBS).…”

Section: Methodsmentioning

confidence: 99%

Immuno-biosensor for Detection of CD20-Positive Cells Using Surface Plasmon Resonance

et al. 2017

Self Cite

View full text Add to dashboard Cite

Purpose: Surface plasmon resonance (SPR) sensing confers a real-time assessment of molecular interactions between biomolecules and their ligands. This approach is highly sensitive and reproducible and could be employed to confirm the successful binding of drugs to cell surface targets. The specific affinity of monoclonal antibodies (MAb) for their target antigens is being utilized for development of immuno-sensors and therapeutic agents. CD20 is a surface protein of B lymphocytes which has been widely employed for immuno-targeting of B-cell related disorders. In the present study, binding ability of an anti-CD20 MAb to surface antigens of intact target cells was investigated by SPR technique.Methods: Two distinct strategies were used for immobilization of the anti-CD20 MAb onto gold (Au) chips. MUA (11-mercaptoundecanoic acid) and Staphylococcus aureus protein A (SpA) were the two systems used for this purpose. A suspension of CD20-positive Raji cells was injected in the analyte phase and the resulting interactions were analyzed and compared to those of MOLT-4 cell line as CD20-negative control.Results: Efficient binding of anti-CD20 MAb to the surface antigens of Raji cell line was confirmed by both immobilizing methods, whereas this MAb had not a noticeable affinity to the MOLT-4 cells.Conclusion: According to the outcomes, the investigated MAb had acceptable affinity and specificity to the target antigens on the cell surface and could be utilized for immuno-detection of CD20-positive intact cells by SPR method.

show abstract

“…Affinity unit depends on equilibrium dissociation constant (K D ) and low values of K D indicate a high tendency of association between two materials that can be calculated through the equation (Eq.) 1 6 : …”

mentioning

confidence: 99%

Tips on ligand immobilization and kinetic study using surface plasmonresonance

Dolatabadi

Guárdia

2016

Bioimpacts

View full text Add to dashboard Cite

Surface plasmon resonance (SPR) technique offers a robust label-free approach applicable in various investigations including binding affinity, specificity and kinetics of biological macromolecules (e.g., peptides, proteins and nucleotidase) and small molecules. SPR provides extremely important data on the kinetics and affinity of substances examined, through which bio-specific interaction(s) can be established by the analysis of adsorption of analyteonto the immobilized ligand(s) on a sensor-based analytical system. Due to SPR wide applications in biomedical laboratories, the aim of this editorial is to highlight the importance of SPR in affinity kinetics and ligand immobilization.

show abstract

Kinetic studies of bovine serum albumin interaction with PG and TBHQ using surface plasmon resonance

Cited by 41 publications

References 40 publications

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

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

Immuno-biosensor for Detection of CD20-Positive Cells Using Surface Plasmon Resonance

Tips on ligand immobilization and kinetic study using surface plasmonresonance

Contact Info

Product

Resources

About