Study on the binding of 2,3-diazabicyclo[2.2.2]oct-2-ene with bovine serum albumin by fluorescence spectroscopy

Anbazhagan, V.; Renganathan, R.

doi:10.1016/j.jlumin.2008.02.004

Cited by 186 publications

(64 citation statements)

References 27 publications

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“…Fluorescence quenching spectra at different temperatures (290, 301 and 310 K) were obtained at an excitation wavelength of 280 nm, with the slit widths of both the excitation and emission set at 5.0 nm and the scanning speed is 1200 nm/min. The fluorescence intensity was corrected for absorption of exciting light and re-absorption of emitted light using the following equation (Anbazhagan and Renganathan, 2008 …”

Section: Fluorescence Spectral Measurementsmentioning

confidence: 99%

Spectroscopic investigation on the food components–drug interaction: The influence of flavonoids on the affinity of nifedipine to human serum albumin

Wang

Liu

et al. 2015

Food and Chemical Toxicology

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Section: Fluorescence Spectral Measurementsmentioning

confidence: 99%

Spectroscopic investigation on the food components–drug interaction: The influence of flavonoids on the affinity of nifedipine to human serum albumin

Wang

Liu

et al. 2015

Food and Chemical Toxicology

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“…BSA has a strong fluorescence emission at 340 nm on exciting at 280 nm (Anbazhagan and Renganathan, 2008). The fluorescence spectra of BSA in the presence of different concentrations of OMT were shown in Fig.…”

Section: Thermodynamic Parameters Analysismentioning

confidence: 99%

Study on the interaction of oxymatrine with bovine serum albumin

Zhu

Sun

et al. 2010

Med Chem Res

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The binding reaction of oxymatrine (OMT) with bovine serum albumin (BSA) was studied by the methods of isothermal titration calorimetry, fluorescence, and circular dichroism (CD) spectroscopy. The thermodynamic results indicated that there were two classes of binding sites on the BSA molecule for OMT molecule. When the drug molecule binding to the first class of sites, the standard changes of enthalpy (DH 1°) and entropy (DS 1°) were (-1.07 ± 0.50) kJ/mol and (98.3 ± 0.50) J/ mol/K, respectively. The possible largest number of binding site (N 1 ) was (10.0 ± 0.20). This type of binding was an enthalpy-entropy synergically driven process. On the second class of binding sites, the standard changes of enthalpy (DH 2°) and entropy (DS 2°) were (1.91 ± 0.03) kJ/ mol and (79.8 ± 0.40) J/mol/K, respectively. The possible largest number of binding site (N 2 ) was (25.0 ± 0.30). This type of binding was entropy driven process. The intrinsic fluorescence of BSA was slightly quenched by the formation of BSA-OMT complex. The CD spectra experiment showed that the a-helix contents of BSA decreased. These revealed that the microenvironment and conformation of BSA were changed in the binding reaction.

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“…32 It is an appropriate way to distinguish dynamic from static quenching mechanism by examining the quenching rate constant. According to the Stern-Volmer linear equation, the quenching rate constant (1.852 × 10 13 L/(M s -1 )) at 298 K is calculated by the slope of the I0/I against [Q] plots.…”

Section: Fluorescence Quenching Studiesmentioning

confidence: 99%

Synthesis and Characterization of TiO2 Nanoparticles: Applications in Research on the Interaction of Colloidal TiO2 with Human Serum Albumin by Fluorescence Spectroscopy

et al. 2012

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Study on the binding of 2,3-diazabicyclo[2.2.2]oct-2-ene with bovine serum albumin by fluorescence spectroscopy

Cited by 186 publications

References 27 publications

Spectroscopic investigation on the food components–drug interaction: The influence of flavonoids on the affinity of nifedipine to human serum albumin

Spectroscopic investigation on the food components–drug interaction: The influence of flavonoids on the affinity of nifedipine to human serum albumin

Study on the interaction of oxymatrine with bovine serum albumin

Synthesis and Characterization of TiO2 Nanoparticles: Applications in Research on the Interaction of Colloidal TiO2 with Human Serum Albumin by Fluorescence Spectroscopy

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