Spectroscopic studies on the interaction of bovine serum albumin with surfactants and apigenin
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Bovine serum albumin
Binding constant
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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Bovine serum albumin
Binding constant
Acceptor
Serum Albumin
Hydrophobic effect
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The binding interaction between the mixed complexes([Cu(Glu·Arg) ]SO4·5H2O) and bovine serum albumin(BSA) was investigated by fluorescence spectroscopy.The mixed complexes was designed and synthesized with Cu(Ⅱ),glutamate(Glu) and arginine(Arg).The mixed complexes have powerful ability to quench the BSA fluorescence via a static quenching mechanism and quenching rate constant is1.2 × 1012L·mol- 1·s- 1and binding constant is 9.7 × 103L/mol and the number of binding site is 0.966.
Bovine serum albumin
Binding constant
Serum Albumin
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The toxic interaction of bisphenol A(BPA) with bovine serum albumin(BSA) was studied by using ?uorescence spectra and UV-vis absorption spectra.The experimental results indicate that the intrinsic fluorescence of BSA can be quenched by the addition of bisphenol A.The quenching mechanism is due to static quenching,and the binding constant is 2.54161×103,and the number of binding sites is 0.655931.The experimental results also show that the binding of bisphenol A to BSA can induce conformational changes to BSA,as shown by the UV–vis spectra.Such conformation changes can induce toxic effects.
Bovine serum albumin
Binding constant
Serum Albumin
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Objective: To investigate the mechanism of interaction between curcumin and bovine serum albumin(BSA).Methods: Fluorescence spectroscopy was used to investigate the interaction between curcumin and BSA on different temperature,The Linewearver-Burk formula was used to process the experiment data.The binging constant and number of binding site were obtained.Results: The fluorescence intensity of BSA was quenched by curcumin,the binding constant(Ka) was large and was less affected by temperature.Conclusions: The mechanism of interaction between curcumin and BSA was a static quenching process.
Bovine serum albumin
Binding constant
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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Bovine serum albumin
Binding constant
Chromophore
Serum Albumin
Acceptor
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The interaction between lornoxicam and bovine serum albumin was studied at pH 7.0 by spectroscopic methods including fluorescence spectra and UV-visible absorption spectra.It showed that the complex formation between bovine serum albumin and lornoxicam resulted in the quenching of the intrinsic fluorescence of bovine serum albumin;The main mechanism of protein fluorescence quenching was a static quenching procedure.The binding site number n and apparent binding constant KA were measured at different temperatures based on Stern-volmer equation.The distance between BSA and lornoxicam was measured at different temperatures based on the Forster nonradiative energy transfer theory.On the basis of the thermodynamic parameters,the main sorts of binding force between lornoxicam and bovine serum albumin could be judged as electrostatic force,synchronous fluorescence and three-dimensional fluorescence spectra were used to investigate the structure change of bovine serum albumin with the addition of lornoxicam.In addition,the effect of some ions on the binding constant of lornoxicam with BSA was also studied.
Lornoxicam
Bovine serum albumin
Binding constant
Serum Albumin
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We report the complexation of bovine serum albumin (BSA) with resveratrol, genistein, and curcumin, at physiological conditions, using constant protein concentration and various polyphenol contents. FTIR, CD, and fluorescence spectroscopic methods were used to analyze the ligand binding mode, the binding constant, and the effects of complexation on BSA stability and conformation. Structural analysis showed that polyphenols bind BSA via hydrophilic and hydrophobic interactions with the number of bound polyphenol (n) being 1.30 for resveratrol-BSA, 1.30 for genistein-BSA, and 1.0 for curcumin-BSA. The polyphenol-BSA binding constants were K(Res-BSA) = 2.52(+/-0.5) x 10(4) M(-1), K(Gen-BSA) = 1.26(+/-0.3) x 10(4) M(-1), and K(Cur-BSA) = 3.33(+/-0.8) x 10(4) M(-1). Polyphenol binding altered BSA conformation with a major reduction of alpha-helix and an increase in beta-sheet and turn structures, indicating a partial protein unfolding.
Bovine serum albumin
Binding constant
Serum Albumin
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The effect of ferric iron(Fe3+) on the interaction between breviscapinun(BR) and bovine serum albumin(BSA) was investigated by means of fluorescence spectrometry and ultraviolet absorption spectrometry.The factors influencing the interaction between BR and BSA were analyzed in relation to the static action and coordination of Fe3+ and BSA as well as the coordination action between Fe3+ and BR.Results indicate that Fe3+ does not change the mechanism for BSA to interact with BR,but it contributes to reduce the quenching constant,binding constant and binding sites of BSA with BR.
Bovine serum albumin
Binding constant
Serum Albumin
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