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ABSTRACT: The interaction between 2,4-dichlorophenol (DCP) and bovine serum albumin (BSA) was investigated by fluorescence spectroscopy
combined with UV-vis absorption and circular dichroism (CD) spectroscopy under simulative physiological conditions. The experiment
results show that the fluorescence intensity of BSA is dramatically decreased owing to the formation of a DCP–BSA complex.
The corresponding effective quenching constants (K
a) between DCP and BSA at four different temperatures (292, 298, 304 and 310K) were determined to be 10.08×104, 9.082×104, 8.177×104, and 7.260×104L⋅mol−1, respectively. The thermodynamics parameters enthalpy change (ΔH) and entropy change (ΔS) were calculated to be −13.64kJ⋅mol−1 and 49.08J⋅mol−1⋅K−1, which suggested that hydrophobic interaction was the predominant intermolecular force. Site marker competitive experiments
indicated that the binding of DCP to BSA primarily takes place in subdomain IIA. The binding distance(r) between DCP and the tryptophan residue of BSA ias 4.09nm according to Förster’s theory of non-radioactive energy transfer.
The conformational investigation demonstrated that the presence of DCP decreased the α-helical content of BSA and induced a slight unfolding of the polypeptides of protein, which confirmed the occurrence some
micro environmental and conformational changes of BSA molecules.
Keywords2,4-Dichlorophenol-Bovine serum albumin-Fluorescence spectrum-Binding site-Circular dichroism
Journal of Solution Chemistry 04/2012; 39(4):495-510. · 1.41 Impact Factor
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ABSTRACT: In this work, fluorescence spectroscopy in combination with circular dichroism spectroscopy and molecular modeling was employed to investigate the binding of 10-hydroxycamptothecin (HCPT) to human serum albumin (HSA) under simulative physiological conditions. The experiment results showed that the fluorescence quenching of HSA by HCPT was a result of the formation of HCPT-HSA complex. The corresponding association constants (K (a)) between HCPT and HSA at four different temperatures were determined according to the modified Stern-Volmer equation. The results of thermodynamic parameters ΔG, ΔH, and ΔS indicated that hydrogen bonds and van der Waals forces played major roles for HCPT-HSA association. Site marker competitive displacement experiment indicated that the binding of HCPT to HSA primarily took place in sub-domain IIA (site I). Molecular docking study further confirmed the binding mode and the binding site obtained by fluorescence and site marker competitive experiments. The conformational investigation showed that the presence of HCPT decreased the α-helical content of HSA and induced the slight unfolding of the polypeptides of protein, which confirmed some micro-environmental and conformational changes of HSA molecules.
Molecular Biology Reports 12/2011; 39(5):5115-23. · 2.93 Impact Factor
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ABSTRACT: The interaction between 4-(4-fluorobenzylideneamino)-5-propyl-4H-1,2,4-triazole-3-thiol (FBTZ) and human serum albumin (HSA) under simulative physiological conditions was investigated by fluorescence, UV-vis absorption and circular dichroism (CD) spectroscopy as well as molecular modeling method. Fluorescence spectroscopic data showed that the fluorescence quenching of HSA was a result of the formation of FBTZ-HSA complex. According to the modified Stern-Volmer equation, the effective quenching constants (K (a)) of FBTZ to HSA were obtained at three different temperatures. The enthalpy change (ΔH) and entropy change (ΔS) were calculated on the basis of van't Hoff equation, and the results showed that hydrogen-bonding and van der Waals forces were the dominant intermolecular forces to stabilize the complex. Site marker competitive replacement experiments demonstrated that the binding of FBTZ to HSA primarily took place in sub-domain IIA (Sudlow's site I). The binding distance (r) between FBTZ and the tryptophan residue of HSA was estimated according to the theory of fluorescence resonance energy transfer. The conformational investigation showed that the presence of FBTZ induced some changes of secondary structure of HSA. Molecular modeling study further confirmed the binding mode obtained by experimental study.
Biological trace element research 10/2011; 143(1):562-78. · 1.92 Impact Factor
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ABSTRACT: The interaction between benzophenone (BP) and bovine serum albumin (BSA) was investigated by the methods of fluorescence spectroscopy combined with UV-Vis absorption and circular dichroism (CD) measurements under simulative physiological conditions. The experiment results showed that the fluorescence quenching of BSA by BP was resulted from the formation of a BP-BSA complex and the corresponding association constants (Ka) between BP and BSA at four different temperatures had been determined using the modified Stern-Volmer equation. The enthalpy change (ΔH) and entropy change (ΔS) were calculated to be -43.73 kJ mol(-1) and -53.05 J mol(-1) K(-1), respectively, which suggested that hydrogen bond and van der Waals force played major roles in stabilizing the BP-BSA complex. Site marker competitive experiments indicated that the binding of BP to BSA primarily took place in site I (sub-domain IIA). The conformational investigation showed that the presence of BP decreased the α-helical content of BSA and induced the slight unfolding of the polypeptides of protein, which confirmed some micro-environmental and conformational changes of BSA molecules.
Molecular Biology Reports 11/2010; 38(4):2445-53. · 2.93 Impact Factor
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ABSTRACT: The effect of cerium on mitochondria isolated from hybrid rice Shanyou 63 (Oryza sativa L) was investigated. Through in vivo culture, low dose Ce3+ promoted, but higher dose Ce3+, restrained mitochondrial heat production. However, through vitro incubation, Ce3+ showed only inhibitory action on mitochondrial energy turnover, the concentration required for 50% inhibition being 46.7 μM. In addition, Ce3+, like Ca2+, induced rice mitochondrial swelling and decreased membrane potential (△ψ), which was inhibited by the specific permeability transition inhibitor cyclosporine A (CsA). The induction approached a constant level while mitochondrial metabolism was fully prevented by Ce3+. These results demonstrated that cerium influenced rice mitochondria in vivo and in vitro via different action pathways, and the latter involved the opening of rice mitochondrial permeability.
Biological trace element research 11/2010; 143(2):1142-8. · 1.92 Impact Factor
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ABSTRACT: Fluorescence spectroscopy in combination with UV-Vis absorption spectroscopy were employed to investigate the binding of an antibacterial drug Ciprofloxacin (CPFX) to bovine serum albumin (BSA) under the physiological conditions. In the discussion of the quenching mechanism, it was proved that the fluorescence quenching of BSA by CPFX is a result of the formation of CPFX-BSA complex. Binding parameters were determined using the modified Stern-Volmer equation and Scatchard equation to provide a measure of the binding affinity between CPFX and BSA. The results of thermodynamic parameters DeltaG, DeltaH, DeltaS, at different temperatures indicate that the electrostatic interactions play a major role for CPFX-BSA association. Site marker competitive experiments indicated that the binding of CPFX to BSA primarily took place in site I. Furthermore, the effect of metal ions to CPFX-BSA system was studied, and the distance r between donor (BSA) and acceptor (CPFX) was obtained according to fluorescence resonance energy transfer (FRET). The conformation of BSA upon CPFX binding was evaluated by measuring synchronous fluorescence properties of the CPFX-BSA complex.
The Protein Journal 05/2010; 29(4):234-41. · 1.04 Impact Factor
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ABSTRACT: The binding of one fluorine including triazole (C(10)H(9)FN(4)S, FTZ) to bovine serum albumin (BSA) was studied by spectroscopic techniques including fluorescence spectroscopy, UV-Vis absorption, and circular dichroism (CD) spectroscopy under simulative physiological conditions. Fluorescence data revealed that the fluorescence quenching of BSA by FTZ was the result of forming a complex of BSA-FTZ, and the binding constants (K (a)) at three different temperatures (298, 304, and 310 K) were 1.516 × 10(4), 1.627 × 10(4), and 1.711 × 10(4) mol L(-1), respectively, according to the modified Stern-Volmer equation. The thermodynamic parameters ΔH and ΔS were estimated to be 7.752 kJ mol(-1) and 125.217 J mol(-1) K(-1), respectively, indicating that hydrophobic interaction played a major role in stabilizing the BSA-FTZ complex. It was observed that site I was the main binding site for FTZ to BSA from the competitive experiments. The distance r between donor (BSA) and acceptor (FTZ) was calculated to be 7.42 nm based on the Förster theory of non-radioactive energy transfer. Furthermore, the analysis of fluorescence data and CD data revealed that the conformation of BSA changed upon the interaction with FTZ.
Biological trace element research 03/2010; 138(1-3):125-38. · 1.92 Impact Factor
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ABSTRACT: Fluorescence spectroscopy in combination with UV-vis absorption spectroscopy was employed to investigate the binding of an important traditional medicinal herb berberine to bovine serum albumin (BSA) under the physiological conditions. In the mechanism discussion, it was proved that the fluorescence quenching of BSA by berberine is a result of the formation of berberine-BSA complex. Fluorescence quenching constants were determined using the Stern-Volmer equation and Scatchard equation to provide a measure of the binding affinity between berberine and BSA. The results of thermodynamic parameters ΔG, ΔH, ΔS at different temperatures indicate that the electrostatic interactions play a major role for berberine-BSA association. Site marker competitive experiments indicated that the binding of berberine to BSA primarily took place in site II. Furthermore, the Effect of supramolecules to berberine-BSA system, and the distance r between donor (BSA) and acceptor (berberine) was obtained according to fluorescence resonance energy transfer (FRET).
Molecular Biology Reports 03/2010; 37(8):3827-32. · 2.93 Impact Factor
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ABSTRACT: The binding interaction of the cobalt(II) 1,10-phenanthroline complex (Co(phen) (3) (2+) , phen = 1,10-phenanthroline) with bovine serum albumin (BSA) was investigated by fluorescence spectroscopy combined with UV-Vis absorption and circular dichroism measurements under simulative physiological conditions. The experiment results showed that the fluorescence intensity of BSA was dramatically decreased owing to the formation of Co(phen) (3) (2+) -BSA complex. The corresponding association constants (K (a)) between Co(phen) (3) (2+) and BSA at four different temperatures were calculated according to the modified Stern-Volmer equation. The enthalpy change (DeltaH degrees ) and entropy change (DeltaS degrees ) were calculated to be -2.73 kJ mol(-1) and 82.27 J mol(-1) K(-1), respectively, which suggested that electrostatic interaction and hydrophobic force played major roles in stabilizing the Co(phen) (3) (2+) -BSA complex. Site marker competitive experiments indicated that the binding of Co(phen) (3) (2+) to BSA primarily took place in site I of BSA. A value of 4.11 nm for the average distance r between Co(phen) (3) (2+) (acceptor) and tryptophan residues of BSA (donor) was derived from Förster's energy transfer theory. The conformational investigation showed that the presence of Co(phen) (3) (2+) resulted in the change of BSA secondary structure and induced the slight unfolding of the polypeptides of protein, which confirmed the microenvironment and conformational changes of BSA molecules.
Biological trace element research 10/2009; 135(1-3):136-52. · 1.92 Impact Factor
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ABSTRACT: Heteropolyoxometalate complexes have been widely applied in many fields. In this paper, the interaction between a series of novel rare earth molybdotungstosilicate heteropolyoxometalates, K(10)H(3)[Ln(SiMo(6)W(5)O(39))(2)].xH(2)O (abbr. LnW(5), Ln = Pr (x = 30), Gd (x = 29), Dy (x = 28), and Yb (x = 31)), and bovine serum albumin (BSA) was investigated by spectroscopic approach under the physiological conditions. In the mechanism discussion, it was proved that the fluorescence quenching of BSA by LnW(5) is a result of the formation of LnW(5)-BSA complex. Fluorescence quenching constants were determined using the Stern-Volmer equation to provide a measure of the binding affinity between LnW(5) and BSA. The binding affinity ranked in the order GdW(5) > DyW(5) > PrW(5) > YbW(5). The results of thermodynamic parameters DeltaG, DeltaH, and DeltaS at different temperatures indicate that van der Waals interactions and hydrogen bonds play a major role for LnW(5)-BSA association. Furthermore, the distance r between donor (BSA) and acceptor (LnW(5)) was obtained according to fluorescence resonance energy transfer.
Biological trace element research 09/2009; 136(1):8-17. · 1.92 Impact Factor
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ABSTRACT: In this paper, the biological activation of heteropoly complex of molybdotungstosilicate containing lanthanum K(10)H(3)La(SiMo(6)W(5)O(39))(2)x26H(2)O (LaW(5)) was investigated by spectroscopic approach and microcalorimetry under the human physiological conditions. Fluorescence spectroscopy in combination with UV-Vis absorption spectroscopy was employed to investigate the binding of LaW(5) to bovine serum albumin (BSA). In the mechanism discussion, it was proved that the fluorescence quenching of BSA by LaW(5) is a result of the formation of LaW(5)-BSA complex. Binding parameters were determined using the Stern-Volmer equation. The results of thermodynamic parameters G, H, S at different temperatures indicate that van der Waals interactions and hydrogen bonds play a major role for LaW(5)-BSA association. The distance r between donor (BSA) and acceptor (LaW(5)) was obtained according to fluorescence resonance energy transfer. Furthermore, the calorimetric method was used to monitor the biological activity of LaW(5) in Escherichia coli.
Biological trace element research 09/2009; 135(1-3):314-24. · 1.92 Impact Factor
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ABSTRACT: The interaction between bovine serum albumin (BSA) and benzidine (BD) in aqueous solution was investigated by fluorescence spectroscopy, circular dichroism (CD) spectra and UV-Vis spectroscopy, as well as resonance light scattering spectroscopy (RLS). It was proved from fluorescence spectra that the fluorescence quenching of BSA by BD was a result of the formation of BD-BSA complex, and the binding constants (K (a)) were determined according to the modified Stern-Volmer equation. The enthalpy change (DeltaH) and entropy change (DeltaS) were calculated to be -34.11 kJ mol(-1) and -25.89 J mol(-1) K(-1), respectively, which implied that van der Waals force and hydrogen bond played predominant roles in the binding process. The addition of increasing BD to BSA solution caused the gradual enhancement in RLS intensity, exhibiting the forming of the aggregate. Moreover, the competitive experiments of site markers suggested that the binding site of BD to BSA was located in the region of subdomain IIA (sudlow site I). The distance (r) between the donor (BSA) and the acceptor (BD) was 4.44 nm based on the Förster theory of non-radioactive energy transfer. The results of synchronous fluorescence and CD spectra demonstrated the microenvironment and the secondary conformation of BSA were changed.
Molecular Biology Reports 06/2009; 37(3):1541-9. · 2.93 Impact Factor
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ABSTRACT: The binding interaction of Congo Red (CGR) with bovine serum albumin (BSA) was investigated by spectroscopic techniques including fluorescence spectroscopy, UV-vis absorption, and circular dichroism (CD) spectroscopy under simulative physiological conditions. Fluorescence data revealed that the fluorescence quenching of BSA by CGR was the result of the formation of a BSA-CGR complex, and the corresponding binding constants (K(a)) at the four different temperatures (292, 298, 304, and 310K) were obtained according to the modified Stern-Volmer equation. The thermodynamic parameters DeltaH and DeltaS were calculated to be -12.67kJmol(-1) and 58.60Jmol(-1)K(-1), respectively, which suggested that both hydrophobic force and hydrogen bond played major roles in stabilizing the BSA-CGR complex. Site marker competitive experiments showed that the binding of CGR to BSA primarily took place in site I of BSA. The distance r between CGR (acceptor) and tryptophan residues of BSA (donor) was calculated to be 3.89nm based on Förster's non-radioactive energy transfer theory. The conformational investigation showed that the presence of CGR resulted in the change of BSA secondary structure and induced the slight unfolding of the polypeptides of protein, which confirmed some micro-environmental and conformational changes of BSA molecules.
Spectrochimica Acta Part A Molecular and Biomolecular Spectroscopy 01/2009; 72(4):907-14. · 2.10 Impact Factor
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ABSTRACT: The interaction between malachite green (MG) and bovine serum albumin (BSA) under simulative physiological conditions was investigated by the methods of fluorescence spectroscopy, UV-vis absorption and circular dichroism (CD) spectroscopy. Fluorescence data showed that the fluorescence quenching of BSA by MG was the result of the formation of the MG-BSA complex. According to the modified Stern-Volmer equation, the effective quenching constants (K(a)) between MG and BSA at four different temperatures were obtained to be 3.734 x 10(4), 3.264 x 10(4), 2.718 x 10(4), and 2.164 x 10(4)L mol(-1), respectively. The enthalpy change (Delta H) and entropy change (DeltaS) were calculated to be -27.25 kJ mol(-1) and -11.23 J mol(-1)K(-1), indicating that van der Waals force and hydrogen bonds were the dominant intermolecular force in stabilizing the complex. Site marker competitive experiments indicated that the binding of MG to BSA primarily took place in sub-domain IIA. The binding distance (r) between MG and the tryptophan residue of BSA was obtained to be 4.79 nm according to Förster theory of non-radioactive energy transfer. The conformational investigation showed that the presence of MG decreased the alpha-helical content of BSA (from 62.6% to 55.6%) and induced the slight unfolding of the polypeptides of protein, which confirmed some micro-environmental and conformational changes of BSA molecules.
Journal of hazardous materials 09/2008; 163(2-3):1345-52. · 4.14 Impact Factor
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ABSTRACT: Under different temperatures and physiological conditions, with cefuroxime axetil concentrations in the range of 1.959 X 10(-6) to 13.71 X 10(-6) mol x L(-1), and bovine serum albumin (BSA) concentrations at 2.0 X 10(-6) mol x L(-1), the interaction between cefuroxime axetil and BSA was studied by fluorescence spectroscopy, three-dimensional fluorescence spectrum, synchronous fluorescence spectrum and UV-Vis absorption spectroscopy. After analyzing and processing the fluorescence quenching data at different temperatures according to Sterm-Volmer equation, Lineweaver-Burk equation and thermodynamic equation, the average value of the apparent binding constant (K(LB): 3.907 X 10(6) L x mol(-1)), and thermodynamics parameters (enthalpy change delta H: -13.43 kJ x mol(-1), entropy change delta S: 81.90 J x K(-1) and standard Gibbs free energy change delta G0: -38.34 kJ x mol(-1)) were calculated, and the amounts of binding sites (n: 1.042)were measured. The fluorescence quenching mechanism of BSA after cefuroxime axetil was added was discussed. BSA was bound with cefuroxime axetil and formed a new compound. The quenching belonged to static fluorescence quenching. The thermodynamic parameters agree with delta H approximately 0, delta S > 0 and delta G0 < 0, and the binding reaction is mainly entropy-driven and electro-static interaction force plays a major role in the reaction. The maximum emission wavelength of Tyr and Trp had an obvious red shift in the synchronous fluorescence spectra, the fluorescence emission wavelength of two peaks had a blue shift in the three-dimensional fluorescence spectrum of BSA in the presence of cefuroxime axetil and the maximum absorbtion wavelenghs of three systems in the UV-Vis absorption spectra were obviously different. These showed that the changes in the micro-environment of Tyr and Trp and demonstrated that the conformation of BSA changed as cefuroxime axetil had been added. This provides important information for discussing the configuration modification of BSA because of the added cefuroxime axetil, and for elucidating the pharmacological effects of cefuroxime axetil and biological effects in the organism.
Guang pu xue yu guang pu fen xi = Guang pu 09/2008; 28(9):2139-43. · 0.84 Impact Factor
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ABSTRACT: The interaction between copper (II) 2-oxo-propionic acid salicyloyl hydrazone (Cu(II)L) and bovine serum albumin (BSA) under physiological conditions was investigated by the methods of fluorescence spectroscopy, UV-Vis absorption, and circular dichroism spectroscopy. Fluorescence data showed that the fluorescence quenching of BSA by Cu(II)L was the result of the formation of the BSA-Cu(II)L complex. The apparent binding constants (K (a)) between Cu(II)L and BSA at four different temperatures were obtained according to the modified Stern-Volmer equation. The thermodynamic parameters, enthalpy change (DeltaH) and entropy change (DeltaS), for the reaction were calculated to be -80.79 kJ mol(-1) and -175.48 J mol(-1) K(-1) according to van't Hoff equation. The results indicated that van der Waals force and hydrogen bonds were the dominant intermolecular force in stabilizing the complex. The binding distance (r) between Cu(II)L and the tryptophan residue of BSA was obtained to be 4.1 nm according to Förster's nonradioactive energy transfer theory. The conformational investigation showed that the application of Cu(II)L increased the hydrophobicity of amino acid residues and decreased the alpha-helical content of BSA (from 62.71% to 37.31%), which confirmed some microenvironmental and conformational changes of BSA molecules.
Biological Trace Element Research 06/2008; 124(3):269-82. · 1.92 Impact Factor
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ABSTRACT: In this work, the interaction between Cu(phen)(2+)(3) and bovine serum albumin (BSA) was investigated by fluorescence spectroscopy combined with UV-vis absorption and circular dichroism (CD) spectroscopic techniques under physiological conditions. The fluorescence data proved that the fluorescence quenching of BSA by Cu(phen)(2+)(3) was the result of the Cu(phen)(2+)(3) -BSA complex formation. The binding constants (K (a)) between Cu(phen)(2+)(3) and BSA at four different temperatures were calculated according to the modified Stern-Volmer equation. The enthalpy change (DeltaH) and entropy change (DeltaS) were calculated to be 10.74 kJ mol(-1) and 54.35 J mol(-1) K(-1), respectively, which indicated that electrostatic interactions played a major role in the formation of Cu(phen)(2+)(3) -BSA complex. The distance r between the donor (BSA) and acceptor[Cu(phen)(2+)(3)] was obtained to be 3.55 nm based on Förster's energy transfer theory. The synchronous fluorescence and CD spectroscopy results showed that the polarity of the residues increased and the lost of the alpha-helix content of BSA (from 59.84 to 53.70%). These indicated that the microenvironment and conformation of BSA were changed in the presence of Cu(phen)(2+)(3).
Biological Trace Element Research 04/2008; 121(3):276-87. · 1.92 Impact Factor
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ABSTRACT: In this paper, the interaction between p-aminoazobenzene (PAAB) and BSA was investigated mainly by fluorescence quenching spectra, circular dichroism (CD) and three-dimensional fluorescence spectra under simulative physiological conditions. It was proved that the fluorescence quenching of BSA by PAAB was mainly a result of the formation of a PAAB-BSA complex. The modified Stern-Volmer quenching constant K(a) and the corresponding thermodynamic parameters DeltaH, DeltaG and DeltaS at different temperatures were calculated. The results indicated that van der Waals interactions and hydrogen bonds were the predominant intermolecular forces in stabilizing the complex. The distance r=4.33 nm between the donor (BSA) and acceptor (PAAB) was obtained according to Förster's non-radioactive energy transfer theory. The synchronous fluorescence, CD and three-dimensional fluorescence spectral results showed that the hydrophobicity of amino acid residues increased and the losing of alpha-helix content (from 63.57 to 51.83%) in the presence of PAAB. These revealed that the microenvironment and conformation of BSA were changed in the binding reaction.
Journal of Fluorescence 02/2008; 18(1):109-18. · 2.11 Impact Factor
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ABSTRACT: At different temperatures, the binding of naphthol green B (NGB) to bovine serum albumin (BSA) was studied by the fluorescence spectroscopy, three-dimensional fluorescence spectrum, synchronous fluorescence spectrum and ultra-violet spectrum. It was shown that this compound has a quite strong ability to quench the fluorescence from BSA. After analyzing the fluorescence quenching data according to Sterm-Volmer equation and Lineweaver-Burk equation, it was found that BSA had reacted with naphthol green B and formed a new compound, the quenching action was due to static fluorescence quenching, and the action force was electrostatic interaction. According to the Lineweaver-Burk equation and thermodynamic equation, the average value of the binding constant (KLe: 1.411 x 10(5) L x mol(-1)), the thermodynamic parameters (DeltaHtheta: -5.707 kJ x mol(-1), DeltaGtheta: -30.25 kJ x mol(-1) and DeltaStheta: 79.95 J x K(-1)) and the amounts of binding sites (1.258) were obtained, providing important information for the research on the configuration modification of BSA because of the added naphthol green B, biological effects in a living body, and the coloration mechanism of naphthol green B.
Guang pu xue yu guang pu fen xi = Guang pu 01/2008; 27(12):2542-5. · 0.84 Impact Factor
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ABSTRACT: The binding of eosin Y to bovine serum albumin (BSA) was studied by fluorescence spectroscopy and ultraviolet spectrum. It was shown that this compound has a quite strong ability to quench the fluorescence from BSA. After analyzing the fluorescence quenching data according to Sterm-Volmer equation, Lineweaver-Burk equation and thermodynamic equation at 298. 15 K, the binding constant(KLB= 3. 601 x 10(5) L x mol(-1)) and thermodynamic parameters (deltaHtheta: - 22. 66 kJ x mol(-1), deltaGtheta: -31. 30 kJ x mol(-1) and deltaStheta: 36.32 J x K(-1)were obtained, which provide important information for researching the configuration modification of BSA caused by added eosin Y, biological effects of eosin Y in a living body, and dyeing mechanism of cells.
Guang pu xue yu guang pu fen xi = Guang pu 01/2007; 26(12):2306-10. · 0.84 Impact Factor
