Fluorescence Spectroscopic Study of Interaction between Olanzapine and Bovine Serum Albumin

Rashid, Mohammad A.; Rabbi, Sikder Nahidul Islam

doi:10.4172/2153-2435.1000408

Cited by 15 publications

(15 citation statements)

References 17 publications

(28 reference statements)

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“…Fluorescence spectroscopy is one of the most convenient and successful methods applied to study drug-protein interactions [13]. Fluorescence measurements provide information on drug-protein interaction such as the quenching mechanism, binding affinity between the drug and protein, binding site for the drug on protein, nature of binding force and the intermolecular distance between the drug and protein molecule [14]. Thus, fluorescence measurements of BSA in the absence and presence of different concentrations of RPG were performed to understand the binding characteristics of RPG-BSA interactions.…”

Section: Resultsmentioning

confidence: 99%

Interaction of repaglinide with bovine serum albumin: Spectroscopic and molecular docking approaches

Pawar

Seetharamappa

2019

Journal of Pharmaceutical Analysis

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Repaglinide (RPG) regulates the amount of glucose by stimulating the pancreas to release insulin in the blood. In view of its biological importance, we have examined the interaction between RPG and a model protein, bovine serum albumin (BSA) employing various spectroscopic, electrochemical and molecular docking methods. Fluorescence spectra of BSA were recorded in the presence and absence of RPG in phosphate buffer of pH 7.4. Fluorescence intensity of BSA was decreased upon the addition of increased concentrations of RPG, indicating the interaction between RPG and BSA. Stern-Volmer quenching analysis results revealed that RPG quenched the intensity of BSA through dynamic quenching mechanism. This was further confirmed from the time-resolved fluorescence measurements. The binding constant as calculated from the spectroscopic and voltammetric results was observed to be in the order of 10 4 M −1 at 298 K, suggesting the moderate binding affinity between RPG and BSA. Competitive experimental results revealed that the primary binding site for RPG on BSA was site II. Absorption and circular dichroism studies indicated the changes in the secondary structure of BSA upon its interaction with RPG. Molecular simulation studies pointed out that RPG was bound to BSA in the hydrophobic pocket of site II.

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Section: Resultsmentioning

confidence: 99%

Interaction of repaglinide with bovine serum albumin: Spectroscopic and molecular docking approaches

Pawar

Seetharamappa

2019

Journal of Pharmaceutical Analysis

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“…It may also driven by hydrogen bonding, van der Waals forces, electrostatic forces and hydrophobic interactions. 35 In case of hydrophobic interactions, both ΔH and ΔS values are positive. These values are negative for interactions driven by van der Waals forces and hydrogen-bond formation in low dielectric media.…”

Section: ■ Results and Discussionmentioning

confidence: 99%

“…The negative value of ΔG implied that the binding process between NPs (COS and CS) and proteins (BSA and HSA) was spontaneous, throughout the interactions. 24,35 All the NP (COS and CS)−BSA complexes showed positive ΔH and ΔS values. This indicated that hydrophobic forces played a major role in the interaction between NPs (COS and CS) and BSA.…”

Section: ■ Results and Discussionmentioning

confidence: 99%

Understanding the Stability of Nanoparticle–Protein Interactions: Effect of Particle Size on Adsorption, Conformation and Thermodynamic Properties of Serum Albumin Proteins

Suvarna

Dyawanapelly

Kansara

et al. 2018

ACS Appl. Nano Mater.

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The present work evaluates the effect of nanoparticle size on the structure and function of albumin proteins. Further, the work evaluates the nature of binding between low molecular weight (∼20 kDa) chitosan oligosaccharide nanoparticles (COS NPs) and high molecular weight (∼85–90 kDa) chitosan nanoparticles (CS NPs) with two model proteins, namely, human serum albumin (HSA) and bovine serum albumin (BSA). The size-dependent pattern of protein-adsorption onto nanoparticle surface was studied using dynamic light scattering and further quantified by size exclusion chromatography-HPLC method. Circular dichroism spectroscopy revealed that both the proteins underwent conformational change upon association with the cationic nanoparticulate systems. Further, fluorescence spectroscopy was used to probe the stability of nanoparticle–protein complexes, by determining the binding constants of nanoparticle to protein and to evaluate the thermodynamic parameters of the interacted proteins. Smaller-sized NPs, in case of both the polymers, exhibited greater protein binding and increased conformational loss in proteins. Also, CS NPs resulted in lesser change in protein structure, thereby indicating a better biocompatibility than COS NPs. This observation was supported by the results of fluorescence spectroscopy, which implicated that the CS NPs (110 nm) formed the most stable, ground-state complex with HSA, which had a binding constant (K b) of 6.76 × 104 M–1. Results from this investigation provide valuable insights into the molecular level interactions taking place at nanobiointerfaces, which can help in engineering stable, nanoscale materials of chitosan biopolymer and will be helpful to understand the nanoparticle toxicity for biomedical applications.

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“…In addition, Van't Hoff graph (electronic supplementary material, figure S10) was used to study the interaction between EY and OBT by plotting ln K b versus 1/ T according to the equation below [ 33 ]

where Δ H ° = enthalpy change, R = universal gas constant = 8.314 J K −1 mol −1 , T is the absolute temperature (°K), Δ S ° = entropy change and K b = binding constant obtained from modified Stern–Volmer plot.…”

Section: Resultsmentioning

confidence: 99%

Section: Reaction Thermodynamicsmentioning

confidence: 99%

Factorial design-assisted spectroscopic determination of oxybutynin hydrochloride

et al. 2021

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In this study, we have developed two facile spectroscopic methods for quantifying oxybutynin (OBT) hydrochloride in its pure form and tablets using design of experiments (DOEs). The spectroscopic methods depended on the ion-pair complex formation between the tertiary amino group in the drug and eosin in 0.2 M acetate buffer of pH 4. Method I involves spectrophotometric measurement of the absorbance of the developed complex at 550 nm and showed linearity through 1.0–10.0 µg ml −1 . Method II involves spectrofluorometric measurement of the quenching influence of OBT on the native fluorescence of eosin (λ excitation/λ emission of 304/548 nm) and showed linearity through 1.0–6.0 µg ml −1 . Critical parameters were identified through preliminary trials and optimized using the DOE. Additionally, the quenching mechanism was investigated and the pathway of the reaction was postulated. The fluorescence quenching constant and thermodynamic parameters were explored using the Stern–Volmer plot and Van't Hoff graph, respectively. Assessments conducted via analytical ecoscale revealed the ‘excellent-greenness’ of the methodology. The two methods have the potentials of being green and fast compared with other reported methods.

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Fluorescence Spectroscopic Study of Interaction between Olanzapine and Bovine Serum Albumin

Cited by 15 publications

References 17 publications

Interaction of repaglinide with bovine serum albumin: Spectroscopic and molecular docking approaches

Interaction of repaglinide with bovine serum albumin: Spectroscopic and molecular docking approaches

Understanding the Stability of Nanoparticle–Protein Interactions: Effect of Particle Size on Adsorption, Conformation and Thermodynamic Properties of Serum Albumin Proteins

Factorial design-assisted spectroscopic determination of oxybutynin hydrochloride

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