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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 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: 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: 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: 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: Rare earth elements (REEs) have beneficial influence on plant growth and are widely used in agriculture practice, but little is known about the behavior of the REEs in mitochondria of plant cell. Thermogenic metabolic curves were determined by the ampoule method at 303 K using a TAM air isothermal microcalorimeter in mitochondria isolated from hybrid rice Liangyoupeijiu (Oryza sativa L.), and the effect of La(III) on its mitochondrial metabolism was investigated. From the obtained heat flux curves, the crucial parameters including as activity recovery rate constant (k) and maximum heat power (P(max)) were determined. Application of La(3+) in concentrations ranging from 0 to 120 microg/ml significantly increased k and P(max) values with the high point reaching 346 and 222% of the control, respectively. Concentrations from 140-150 microg/ml had the opposite effect. These results were consistent with previous reports on the effects of REEs on plant growth. It was concluded that the La-induced change of mitochondrial metabolic activity is a possible mechanism by which La(III) ions influences hybrid rice growth.
Chemistry & Biodiversity 01/2009; 5(12):2684-9. · 1.80 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: Rare earth elements (REEs) have beneficial influence on plant growth and are widely used in agriculture practice, but little is known about behavior of the REEs on mitochondria in plant cells. Thermogenic metabolic curves were determined by the ampoule method at 303 K using a TAM air isothermal microcalorimeter in mitochondria isolated from indice rice 9311 (Oryza sativa L.), and the effect of Ce(III) on mitochondrial metabolism was investigated. By analyzing the obtained heat flux curves, the crucial parameters such as activity recovery rate constant (k) and maximum heat power (P(m)) were investigated. Application of Ce3+ in concentrations ranging from 0 to 120 microg/ml significantly increased k and P(m) values, with the maximum reaching 261 and 180% of the control, respectively. Concentrations from 140 to 150 microg/ml had the opposite effect. These results were consistent with previous reports on the effects of REEs on plant growth. It was concluded that the Ce(III)-induced change of mitochondrial metabolic activity is a possible mechanism by which Ce(III) influenced indice rice 9311 growth.
Chemistry & Biodiversity 07/2008; 5(7):1321-6. · 1.80 Impact Factor
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ABSTRACT: Under the simulated physiological condition of an animal body, the interaction between N′-(1-carboxyethylidene)salicylhydrazide (CESH) and bovine serum albumin (BSA) was investigated by fluorescence spectra, UV-Vis absorption spectra and circular dichroism (CD) spectra. The experiment results showed that the fluorescence of BSA was strongly quenched by CESH because of the formation of a CESH-BSA complex, indicating a static quenching mechanism in the binding process. The modified Stern-Volmer quenching constants (Ka) were 11.23×104, 7.103×104, 4.934×104 and 2.495×104 L·mol−1 at 292, 298, 304 and 310 K, respectively. The thermodynamic parameters ΔG, ΔH and ΔS at the four temperatures were calculated according to van't Hoff equation and the results indicated that hydrogen bonds and van der Waals force played major roles in stabilizing the CESH-BSA complex. The distance r=4.26 nm between the donor BSA and acceptor CESH was obtained according to F?rster's non-radiative energy transfer theory. The synchronous fluorescence spectral results indicated that the hydrophobicity of tyrosine residue increased while the microenvironment around tryptophan residue had no change. The CD and three-dimensional fluorescence spectral results showed that in the presence of CESH, the α-helix content of BSA decreased and the microenvironment and conformation of BSA changed.
Chinese Journal of Chemistry 06/2008; 26(6):1023 - 1029. · 0.75 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: The heat flux of Tetrahymena thermophila BF5 during growth and the effects of La(3+) and Ca(2+) on them were investigated with microcalorimetry; simultaneously, morphological changes of T. thermophila were obtained by light microscope. La(3+) in low concentration (0-5.0 x 10(-4) mol/l) remarkably stimulated T. thermophila metabolism, but high dose of La(3+) (5.8-8.6 x 10(-4) mol/l) restrained it in a linear manner with IC(50) being 7.2 x 10(-4) mol/l. In contrast, low concentration of Ca(2+) did not manifest obvious stimulation on T. thermophila metabolism; moreover, the IC(50) of Ca(2+) was much higher than that of La(3+). Low concentration of La(3+) did not lead to changes in appearance of T. thermophila, but low dose of Ca(2+) clearly promoted the cell proliferation. In addition, the morphological changes of T. thermophila evoked by high concentrations of La(3+) and Ca(2+) were consistent with relevant microcalorimetric results. It is concluded that La and Ca influence T. thermophila via different pathways, and La represents toxic action rather than Ca analogy.
Biological Trace Element Research 06/2008; 122(2):148-56. · 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: Thermogenic metabolic curves were determined by the ampoule method at 303 K using a TAM air isothermal microcalorimeter in mitochondria isolated from rice 9311 (Oryza sativa L). From the thermogenic curves the activity recovery rate constant k and the maximum heat power Pm were obtained. Both were positively correlated to the protein content of rice mitochondria. The corresponding correlation coefficients were 0.9959 and 0.9950, respectively, indicating that the in vitro metabolic activity of mitochondria can be reliably expressed by these parameters. Addition of La (III) ions in concentrations ranging from 0 to 130 microg/mL resulted in significantly higher k and Pm values. Concentrations from 140 to 180 microg/mL had the opposite effect. These results are consistent with previous reports on the effects of rare earth elements on plant growth. We propose that the lanthanum-induced change of mitochondrial metabolic activity is a possible mechanism by which La (III) ions influence indica rice 9311 growth.
Biological Trace Element Research 02/2008; 121(1):60-8. · 1.92 Impact Factor
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ABSTRACT: A microcalorimeric technique was used to evaluate the influence of rare earths Ce3+ on Halobacterium halobium R1 growth. By means of TAM air Thermal Activity Monitor, the thermogenic curves of H. halobium R1 growth were obtained. To analyze the results, the growth rate constant k and IC50 were calculated, indicating that the values of k are linked to the concentration of Ce3+. The growth rate constant k of H. halobium R1 decreased gradually in the low concentration; thus, rare earths restrained the growth of H. halobium R1. On the contrary, as the concentration of Ce3+ became higher, the value of k for H. halobium R1 increased gradually, which showed Ce3+ stimulated the growth of H. halobium R1. When the concentration of rare earths became much higher, the value of k for H. halobium R1 also decreased, and the growth of H. halobium R1 was restrained totally in the end. By using transmission electron microscopy (TEM), it was observed that the transforming of H. halobium R1 in the different concentrations of Ce3+ confirmed the results derived from microcalorimetry. According to the thermogenic curves and TEM photos of H. halobium R1 under various conditions, it showed that there was some special effect about the interaction between rare earths and H. halobium R1 growth.
Biological Trace Element Research 02/2008; 121(1):87-95. · 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: The interactions between loratadine and bovine serum albumin (BSA) and human serum albumin (HSA) were studied using tryptophan fluorescence quenching method. The fluorescence intensity of the two serum albumins could be quenched 70% at the molar ratio [loratadine]:[BSA (or HSA)]=10:1. In the linear range (0-50 micromol L(-1)) quenching constants were calculated using Stern-Volmer equation. Temperature in the range 298 K-310 K had a significant effect (p<0.05) on the two serum albumins through ANOVA analysis and t-test. Furthermore the conformation changes in the interactions were studied using FTIR spectroscopy.
Journal of Biochemical and Biophysical Methods 09/2007; 70(5):743-7. · 2.33 Impact Factor
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ABSTRACT: The interaction of lanthanum(III) 2-oxo-propionic acid salicyloyl hydrazone complex (La(III)L(2)) with bovine serum albumin (BSA) was studied under physiological conditions. Fluorescence spectroscopy in combination with UV-vis absorption and circular dichroism (CD) spectroscopy were used to investigate the binding mechanism, binding constants and conformational changes of BSA in the presence of La(III)L(2). It was found that the fluorescence quenching of BSA by La(III)L(2) resulted mainly from the formation of a La(III)L(2)-BSA complex. The enthalpy change (delta H) and entropy change (deltaS) were found to be -41.03 kJ/mol and -32.61 J/mol/K, respectively, which indicated that van der Waals' interactions and hydrogen bonds were the predominant intermolecular force in stabilizing the complex. The distance r between the donor (BSA) and acceptor (La(III)L(2)) was found to be 4.35 nm, according to Förster theory of non-radioactive energy transfer. Moreover, the conformational changes of BSA by La(III)L(2) were analysed by means of synchronous fluorescence spectra, CD and three-dimensional fluorescence spectra. The experiment results confirmed some microenvironmental and conformational changes of BSA molecules in the presence of La(III)L(2).
Luminescence 23(3):150-6. · 1.73 Impact Factor
