Studies on the antagonistic action between chloramphenicol and quinolones with presence of bovine serum albumin by fluorescence spectroscopy

Liu, Baosheng; Zhao, Fei; Cheng, Xue; Wang, Jing; Lü, Yunkai

doi:10.1016/j.jlumin.2009.12.014

Cited by 44 publications

(17 citation statements)

References 17 publications

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“…Because the quantum yield of phenylalanine is very low and the fluorescence of tyrosine is almost totally quenched, the intrinsic fluorescence of BSA is almost entirely due to tryptophan. By analyzing the fluorescence spectrum [10], we can obtain information about the interactions between BSA and Ce 3+ such as the quenching mechanism, binding constant, and binding sites.…”

Section: Resultsmentioning

confidence: 99%

Study on the binding of cerium to bovine serum albumin

Yuan

Shen

Liu

et al. 2011

J Biochem & Molecular Tox

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The interaction of Ce(3+) to bovine serum albumin (BSA) has been investigated mainly by fluorescence spectra, UV-vis absorption spectra, and circular dichroism (CD) under simulative physiological conditions. Fluorescence data revealed that the quenching mechanism of BSA by Ce(3+) was a static quenching process, the binding constant is 6.70 × 10(5) , and the number of binding site is 1. The thermodynamic parameters (ΔH = -29.94 kJ mol(-1) , ΔG = -32.38 kJ mol(-1) , and ΔS = 8.05 J mol(-1) K(-1) ) indicate that electrostatic effect between the protein and the Ce(3+) is the main binding force. In addition, UV-vis, CD, and synchronous fluorescence results showed that the addition of Ce(3+) changed the conformation of BSA.

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Section: Resultsmentioning

confidence: 99%

Study on the binding of cerium to bovine serum albumin

Yuan

Shen

Liu

et al. 2011

J Biochem & Molecular Tox

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“…Both of the results indicate that the hydrophobicity decreased and the peptide strands of BSA became more extended. Therefore, the binding between La 3 þ and BSA leads to changes in the BSA conformation [22,23].…”

Section: Resultsmentioning

confidence: 99%

“…(4)) at T 1 and T 2 , and R is the universal gas constant. DG and DS are the free-energy change and the entropy change of the binding reaction, respectively [22].…”

Section: The Interaction Forces Between La 3 þ and Bsamentioning

confidence: 99%

Study on the interaction of La3+ with bovine serum albumin at molecular level

Yuan

Shen

Liu

et al. 2011

Journal of Luminescence

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“…The molecular interactions between quinolones and bovine serum albumin (BSA) have been investigated successfully in our previous work. 8,9 The major binding mode of sinafloxacin with ct-DNA has been investigated. 10 As far as we know, the interaction between MOX and ct-DNA has not been investigated.…”

Section: −7mentioning

confidence: 99%