Investigation on the binding behavior between BSA and lenvatinib with the help of various spectroscopic and in silico methods
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Lenvatinib
Bovine serum albumin
Hydrophobic effect
Investigation of Interaction between Platinum Nanoparticles and Bovine Serum Albumin by Spectroscopy
The interaction between platinum manoparticles(PtNP)and bovine serum albumin(BSA)was studied by fluorescence spectroscopy and UV-Vis absorption spectroscopy.The results showed that PtNP caused the fluorescence quenching of BSA through a static quenching procedure.The binding constant(K≈104)and binding site(n≈1)between PtNP and BSA were obtained.According to the values of thermodynamic functions,the type of force between PtNP and BSA was hydrophobic interaction.At the same time,the effect of PtNP on the conformation of BSA was investigated by using synchronous fluorescence spectroscopy.
Bovine serum albumin
Binding constant
Platinum nanoparticles
Ultraviolet visible spectroscopy
Hydrophobic effect
Serum Albumin
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The binding characteristics of 2-(p-aminobenzene)-3,3-dimethyl-3H-indole(A) and bovine serum albumin(BSA) was studied by fluorescence spectroscopy in aqueous solution.The combination constants K=1.82×105L/mol.The binding distance(r=2.34nm) between A and BSA and the energy transfer efficiency were obtained based on Foester spectroscopy theory for energy transfer.The effect of A on the conformation of BSA was further analyzed by using synchronous fluorescence spectrometry.
Bovine serum albumin
Serum Albumin
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The binding reaction between Tetrabromofluorescein,Tetrachloro-tetrabromofluorescein,diiodofluorescein,Ethylrhodamine B,Janus green B with bovine serum albumin(BSA) in aqueous solution was studied by fluorescence and ultraviolet-visible absorption spectra.The results show that hydrophobic force plays the decisive role and electrostatic force on the secondary role in the reactions.In contrast,bovine serum albumin can most firmly combine with anions,secondly with neutral molecules,finally for the cations.The fluorescent probes insert their common nonpolar phenyl into hydrophobic cavity of BSA through hydrophobic force where they finally combine to tryptophanyl and the formation of weak hydrogen bonds strengthen the action and makes energy transfer efficiency improved significantly.Because of the polar and spacial effects their polar parts can not enter to the cavity,so the reactions all take place by nearly 1∶1 manner.
Bovine serum albumin
Hydrophobic effect
Serum Albumin
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Bovine serum albumin
Serum Albumin
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The interaction of tribromethane and chloroform with bovine serum albumin(BSA)was investigated by using fluorescence spectroscopy and ultraviolet absorption spectroscopy methods.Tribromethane and chloroform statically quenched intrinsic fluorescence of BSA,and tribromethane had stronger binding affinity to BSA than chloroform.Fe3+,Al3+and polypropylene also individually quench fluorescence intensity of BSA,and the binding strength with BSA is polypropyleneFe3+Al3+.The presence of Fe3+,Al3+ and polypropylene can reduce the binding constant of BSA-CHCl3 and BSA-CHBr3,and the order of the action in reducing binding constant is Al3+polypropyleneFe3+.
Bovine serum albumin
Binding constant
Polypropylene
Ultraviolet visible spectroscopy
Fluorescence spectrometry
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Study of the Interaction between Bovine Serum Albumin and Ligustrazine with Spectroscopic Techniques
ABSTRACT The interaction between bovine serum albumin and ligustrazine was studied by fluorescence spectroscopy, synchronous fluorescence spectroscopy, UV-visible absorption spectroscopy, and circular dichroism spectroscopy. The results indicated that the hydrophobic force was the dominant intermolecular force in stabilizing the complex, and the probable quenching mechanism of the bovine serum albumin–ligustrazine interaction was initiated by complex formation. Also, the reaction was determined to be spontaneous. The effect of ligustrazine on the conformation of bovine serum albumin was analyzed using synchronous fluorescence and circular dichroism. The effects of seven metal ions on the binding properties of ligustrazine with bovine serum albumin were discussed.
Bovine serum albumin
Serum Albumin
Hydrophobic effect
Ultraviolet visible spectroscopy
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ABSTRACT The interaction of aspirin with bovine serum albumin was studied at different temperatures using fluorescence quenching and synchronous fluorescence methods. The results indicated that aspirin could quench the intrinsic fluorescence of bovine serum albumin through a static quenching process; the electrostatic interaction contributes to the binding reaction between aspirin and bovine serum albumin. The order of magnitude of binding constants was 103, and the primary binding site for aspirin was found to be sub-hydrophobic domain IIA of bovine serum albumin. The results obtained by the two methods were consistent, which indicated synchronous fluorescence spectrometry was a new method of studying the binding mechanism between drug and protein, and it was a useful supplement to the conventional method.
Bovine serum albumin
Serum Albumin
Fluorescence spectrometry
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The interaction between enoxacin and bovine serum albumin in physiological solution was studied using fluorescence spectroscopy.It was shown that the fluorescence intensity of bovine serum albumin could be apparently quenched by enoxacin based on static quenching model.The binding of enoxacin and bovine serum albumin was principally performed by means of the hydrophobic force.In addition,the competing reaction for bovine serum albumin between Fe(Ⅲ) and enoxacin was discussed,and the effect of Fe(Ⅲ) concentrations on the binding for enoxacin and bovine serum albumin has also been illustrated.
Enoxacin
Bovine serum albumin
Serum Albumin
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The interactions between Theophylline and bovine serum albumin(BSA) were studied by fluorescence and UV absorption spectroscopy.The binding constants KA(1.96×104,3.80×104,1.57×105) and binding sites n(1.0,1.1,1.2) were measured at different temperatures of 10 ℃,28 ℃ and 40 ℃.The results revealed that Theophylline has strong ability to quench the intrinsic fluorescence of BSA and the interactions has been verified as static quenching procedure.According themodynamic parameters the acting forces were determined to be hydrophobic force.
Bovine serum albumin
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The interaction between Hg(Ⅱ) and Bovine Serum Albumin (BSA) was investigated by Fluorescence Spectroscopy in pH=7.15 buffer solution and ionic strength of 0.15mol/L sodium chloride solution.It was proved that static quenching exits between Hg(Ⅱ) and BSA. The results showed that the number of binding sites is n=2 and the combination constant is K=2.468×1010L2·mol-2.
Bovine serum albumin
Buffer solution
Binding constant
Serum Albumin
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