Study on the thermodynamic characteristics between fluoroquinolone and bovine serum albumin

Guo, Ming; Lü, Wei-Jun; Yi, Pinggui; Q, Yu

doi:10.1016/j.jct.2006.08.006

Cited by 9 publications

(3 citation statements)

References 29 publications

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“…Previous studies of fluoroquinolones binding to albumins show a 1:1 interaction between ligands and serum albumins, with moderate affinity and inducing conformational changes in the secondary structure of albumins, as revealed by CD spectra. OFLX forms 1:1 complexes with bovine serum albumin (BSA), with binding constants of the order of 10 4 –10 5 mol/L .…”

Section: Introductionmentioning

confidence: 85%

Study of the interaction between ofloxacin and human serum albumin by spectroscopic methods

2011

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The binding of ofloxacin (OFLX) to human serum albumin (HSA) was investigated by fluorescence and circular dichroism (CD) techniques. The binding parameters have been evaluated by a fluorescence quenching method. Competitive binding measurements were performed in the presence of warfarin and ibuprofen and suggest binding to the warfarin site I of HSA. The distance r between donor (HSA) and acceptor (OFLX) was estimated according to the Forster's theory of non-radiatiative energy transfer. CD spectra revealed that the binding of OFLX to HSA induced conformational changes in HSA. Molecular docking was performed and shows that for the lowest energy complex OFLX is located in site I of HSA, which correlate to the competitive binding experiments.

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Section: Introductionmentioning

confidence: 85%

Study of the interaction between ofloxacin and human serum albumin by spectroscopic methods

2011

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“…Ciprofloxacin hydrochloride (CPFX, the structure is shown in Figure 1) which belongs to the third-generation synthetics of quinolones shows striking potency against enteric Gram-negative bacilli, lesser activity against nonenteric Gram-negative bacilli and staphylococci, and generally marginal activity against streptococci and anaerobes [7,8]. It has received much attention because of its broad-spectrum pharmacological activities and extensive biological effects.…”

Section: Introductionmentioning

confidence: 99%

Investigation on the Competition Interaction of Synthetic Food Colorants and Ciprofloxacin Hydrochloride with Bovine Serum Albumin by Fluorescence Spectroscopy

Liu

Yang

Wang

et al. 2011

Journal of Thermodynamics

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The effects of synthetic food colorants like tartrazine (TTZ), sunset yellow (SY), and erythrosine (ETS) on the binding reaction between ciprofloxacin hydrochloride (CPFX) and bovine serum albumin (BSA) were investigated by fluorescence spectroscopy in the aqueous solution of pH = 7.40. Results showed that CPFX caused the fluorescence quenching of BSA through a static quenching procedure and the primary binding site was located at subdomain IIA of BSA (site I). According to the calculated thermodynamic parameters, it confirmed that CPFX bound to BSA by electrostatic interaction. In addition, the colorants affected the formation of BSA-CPFX complex. This resulted in an increase of the free, biological active fraction of CPFX. The binding distance of BSA-CPFX systems was evaluated according to Förster's theory. Results suggested that the binding distance were increased in the presence of synthetic food colorants.

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“…(Yan et al 2006). Research on the interaction between NFLX and BSA or CHL with BSA has been reported (Guo et al 2007;Kandagal et al 2007;Ding et al 2009), but research on the two drugs coexisting with BSA has not been reported. Research on the interaction of two drugs coexisting has certain theoretical significance for rational usage of drugs.…”

Section: Introductionmentioning

confidence: 99%

Studies on the Antagonistic Action Between Chloramphenicol and Norfloxacin by Fluorescence Spectrum

et al. 2010

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Chloramphenicol (CHL) and Norfloxacin (NFLX) can both quench the fluorescence of bovine serum albumin (BSA) in the aqueous solution of pH ¼ 7.40. This quenching effect becomes more significant when Chloramphenicol and Norfloxacin coexist. Based on this, further studies on the interactions between Chloramphenicol and Norfloxacin using fluorescence spectrum are established. The results showed that the interaction between the drugs would increase the binding constant and binding stability of the drug and protein, thus reducing the free drug concentration. This phenomenon indicates that there exists antagonistic action between drugs. Studies utilizing synchronous spectra showed that the antagonistic action between the drugs would affect the conformation of BSA.

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Study on the thermodynamic characteristics between fluoroquinolone and bovine serum albumin

Cited by 9 publications

References 29 publications

Study of the interaction between ofloxacin and human serum albumin by spectroscopic methods

Study of the interaction between ofloxacin and human serum albumin by spectroscopic methods

Investigation on the Competition Interaction of Synthetic Food Colorants and Ciprofloxacin Hydrochloride with Bovine Serum Albumin by Fluorescence Spectroscopy

Studies on the Antagonistic Action Between Chloramphenicol and Norfloxacin by Fluorescence Spectrum

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