Binding of several anti-tumor drugs to bovine serum albumin: Fluorescence study

Bi, Shuyun; Sun, Ya‐Guang; Qiao, Chunyu; Zhang, Hanqi; Liu, Chunming

doi:10.1016/j.jlumin.2008.12.010

Cited by 138 publications

(75 citation statements)

References 33 publications

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“…(2)) at T 1 and T 2 , and R is the universal gas constant [19,20]. We calculated that H, G, and S were −29.94 kJ mol −1 , −32.38 kJ mol −1 , and 8.05 J mol −1 K −1 , respectively.…”

Section: The Interaction Forces Betweenmentioning

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: The Interaction Forces Betweenmentioning

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 mechanisms of these processes are usually classified as either dynamic or static quenching, which can be distinguished by fluorescence measurements at different temperatures [17]. Dynamic quenching generally depends on molecular diffusion, of which the bimolecular quenching constants are expected to increase with increasing temperature because larger diffusion coefficients are obtained at higher temperatures.…”

Section: Mechanism Of Fluorescence Quenchingmentioning

confidence: 99%

“…For the static quenching interaction, if similar and independent binding sites in BSA were assumed, the binding constants and numbers of binding site can be obtained by the double logarithm regression curve [17],…”

Section: Binding Constants and Binding Sitesmentioning

confidence: 99%

Study of in vitro interaction between tetrabromobisphenol A and bovine serum albumin by fluorescence spectroscopy

Qian

Cui

et al. 2011

Enviro Toxic and Chemistry

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The interaction between tetrabromobisphenol A (TBBPA) and bovine serum albumin (BSA) in simulated physiological conditions (pH = 7.4) was investigated by fluorescence spectroscopy. The results revealed that TBBPA caused the fluorescence quenching of BSA through a static quenching procedure. The binding constants (K) of TBBPA with BSA at 277, 298, and 310 K were obtained as 4.75 × 10(5) L/mol, 5.63 × 10(5) L/mol, and 6.66 × 10(5) L/mol, respectively. There may be two binding sites of TBBPA on BSA. The enthalpy change (ΔH), free energy change (ΔG), and entropy change (ΔS) of thermodynamic parameters indicated that the interaction between TBBPA and BSA was driven mainly by hydrophobic and electrostatic forces. Synchronous fluorescence spectra showed TBBPA binding slightly changed the conformation of BSA by decreasing its polarity and increasing its hydrophobicity. The results of the present study may provide valuable information for studying the distribution and toxicity mechanisms of TBBPA in vivo.

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“…[9][10][11] In order to analyze the effects of hydrophobic molecules on proteins, albumin and firefly luciferase have been widely used as model proteins for the binding behavior and inhibition of protein functions, respectively. [12][13][14][15][16][17][18][19][20][21][22] Recently, we reported that the bacterial luciferase (BL) extracted from marine luminescent bacteria can be utilized to study the effects of hydrophobic molecules on protein functions. 23,24 The luminescence reaction of BL is expressed by the following equation: 25 FM NH2 + CnCHO + O2 → BL FMN + CnCOOH + H2O + hν, (1) where FMNH2, FMN, CnCHO and CnCOOH are the reduced and oxidized forms of flavin monocleotide, substrate n-alkyl aldehyde and corresponding fatty acid, respectively.…”

Section: Introductionmentioning

confidence: 99%

Inhibition of Electrochemically Controlled Bioluminescence of Bacterial Luciferase by n-Alkyl Alcohols

2011

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An electrochemical system has been developed in order to assay the effect of hydrophobic molecules on the bioluminescence of bacterial luciferase (BL). The inhibition of BL luminescence by the long-chain n-alkyl alcohol has been examined using this system. The 1-heptanol, 1-octanol, 1-nonanol, 1-decanol, 1-undecanol and 1-dodecanol inhibited the BL reaction in a dose-dependent manner. The IC50 value, that is, the inhibitor concentration required to decrease the luminescence intensity by half, of these alcohols decreased with increasing the alkyl chain-length of the alcohols. In contrast, the shorter chain 1-hexanol did not inhibit the BL luminescence at all in the examined concentration range. These results indicate that the molecular size and hydrophobicity of the n-alkyl alcohol are the key factors to the inhibitory potency of the BL reaction. The IC50 values are in agreement with values obtained for the bioluminescence of the firefly luciferase system. The proposed electrochemical BL luminescence system will be used for an inhibitory assay of hydrophobic drugs, such as general anesthetics on protein functions.

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Binding of several anti-tumor drugs to bovine serum albumin: Fluorescence study

Cited by 138 publications

References 33 publications

Study on the binding of cerium to bovine serum albumin

Study on the binding of cerium to bovine serum albumin

Study of in vitro interaction between tetrabromobisphenol A and bovine serum albumin by fluorescence spectroscopy

Inhibition of Electrochemically Controlled Bioluminescence of Bacterial Luciferase by n-Alkyl Alcohols

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