Studies on Binding Parameters of Chloramphenicol on Bovine Serum Albumin (BSA)

Alam, SM Mahbubul; Yeasmin, Lucky; Reza, Mahin; Shilpi, Jamil Ahmad; Ahmed, Firoj; ., M. Jamil Akter

doi:10.3923/jbs.2004.203.206

Cited by 4 publications

(3 citation statements)

References 8 publications

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“…11,12,15 The results obtained by this analysis suggest that both sulfamethoxazole and diclofenac sodium have two types of association constants namely high affinity association constant (k 1 ) with low capacity (n 1 ) and low affinity association constant (k 2 ) with high capacity (n 2 ). Sulfamethoxazole is characterized by a k 1 to BSA and the value at pH 7.4 is 29±0.20×10 6 M -1 while k 2 is 1.13±0.20×10 6 M -1 which is nearly 26 times lower than that of k 1 .…”

Section: Estimation Of Binding Parametersmentioning

confidence: 94%

“…The aim of this project was to understand protein binding parameters of concurrently used sulfamethoxazole and diclofenac sodium on bovine serum albumin (BSA) adopting equilibrium dialysis. 11,12 Materials and Methods Equilibrium dialysis method was employed in this study according to the method of Uddin et al 12 and Singlas.…”

Section: Research Articlementioning

confidence: 99%

“…Here, as site-I specific probe, warfarin sodium and site-II specific probe, diazepam were used. 11,12,15 To characterize the binding site of sulfamethoxazole, the free concentration of warfarin sodium (site-I specific probe) bound to BSA was measured upon the addition of sulfamethoxazole. It was found that, the free concentration of warfarin sodium was increased from 100% (as % of initial) to 238.5% when the ratio of sulfamethoxazole to BSA was increased from 0 to 6 ( Figure 3).…”

Section: Identification and Characterization Of Binding Sitementioning

confidence: 99%

See 2 more Smart Citations

Characterization of the Effect of Drug-Drug Interaction on Protein Binding in Concurrent Administration of Sulfamethoxazol and Diclofenac Sodium Using Bovine Serum Albumin

et al. 2016

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Section: Estimation Of Binding Parametersmentioning

confidence: 94%

Section: Research Articlementioning

confidence: 99%

Section: Identification and Characterization Of Binding Sitementioning

confidence: 99%

See 1 more Smart Citation

Characterization of the Effect of Drug-Drug Interaction on Protein Binding in Concurrent Administration of Sulfamethoxazol and Diclofenac Sodium Using Bovine Serum Albumin

et al. 2016

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Comparison of various capillary electrophoretic approaches for the study of drug–protein interaction with emphasis on minimal consumption of protein sample and possibility of automation†

Michalcová

Glatz

2014

J of Separation Science

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The binding ability of a drug to plasma proteins influences the pharmacokinetics of a drug. As a result, it is a very important issue in new drug development. In this study, affinity capillary electrophoresis, capillary electrophoresis with frontal analysis, and Hummel Dreyer methods with internal and external calibration were used to study the affinity between bovine serum albumin and salicylic acid. The binding constant was measured by all these approaches including the equilibrium dialysis, which is considered to be a reference method. The comparison of results and other considerations showed the best electrophoretic approach to be capillary electrophoresis-frontal analysis, which is characterized by the high sample throughput with the possibility of automation, very small quantities of biomacromolecules, simplicity, and a short analysis time. The mechanism of complex formation was then examined by capillary electrophoresis with frontal analysis. The binding parameters were determined and the corresponding thermodynamic parameters such as Gibbs free energy ΔG(0), enthalpy ΔH(0), and entropy changes ΔS(0) at various temperatures were calculated. The results showed that the binding of bovine serum albumin and salicylic acid was spontaneous, and that hydrogen bonding and van der Waals forces played a major role in the formation of the complex.

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Analysis of conjugation of chloramphenicol and hemoglobin by fluorescence, circular dichroism and molecular modeling

Ding

Liu

Sun

et al. 2012

Journal of Molecular Structure

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Studies on Binding Parameters of Chloramphenicol on Bovine Serum Albumin (BSA)

Cited by 4 publications

References 8 publications

Characterization of the Effect of Drug-Drug Interaction on Protein Binding in Concurrent Administration of Sulfamethoxazol and Diclofenac Sodium Using Bovine Serum Albumin

Characterization of the Effect of Drug-Drug Interaction on Protein Binding in Concurrent Administration of Sulfamethoxazol and Diclofenac Sodium Using Bovine Serum Albumin

Comparison of various capillary electrophoretic approaches for the study of drug–protein interaction with emphasis on minimal consumption of protein sample and possibility of automation†

Analysis of conjugation of chloramphenicol and hemoglobin by fluorescence, circular dichroism and molecular modeling

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