Study on the Synergism Effect of Lomefloxacin and Ofloxacin for Bovine Serum Albumin in Solution by Spectroscopic Techniques

Both lomefloxacin (LOM) and ofloxacin (OFL) have a powerful ability to quench the fluorescence of bovine serum albumin (BSA). The fluorescence quenching action is much stronger when the two drugs coexist. The synergism between LOM and OFL was studied using fluorescence and ultraviolet spectroscopy under imitated physiological conditions. The results show that static quenching and non-radiation energy transfer are the main reasons for the fluorescence quenching. The synergism results in both the reduction of the binding stability between drugs and BSA and an increase of the free drug concentration, which will increase the efficacy of drugs. The thermodynamic parameters at different temperatures were calculated and the binding distances r between the drugs and BSA were obtained based on Försters theory of non-radiation energy transfer. The synchronous fluorescence spectra indicated that the effect of synergism affected the conformation of BSA.     

Spectroscopic Studies on the Interaction of 2,4-Dichlorophenol with Bovine Serum Albumin

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 310 K) were determined to be 10.08×10⁴, 9.082×10⁴, 8.177×10⁴, and 7.260×10⁴ L?mol^?1, respectively. The thermodynamics parameters enthalpy change (ΔH) and entropy change (ΔS) were calculated to be ?13.64 kJ?mol^?1 and 49.08 J?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 4.09 nm 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.     

Interaction of Surface-active Fluorescence Probes with Bovine Serum Albumin

The binding between three surface-active substituted 3H-indole fluorescence probes and bovine serum albumin (BSA) in aqueous solution was studied using fluorescence quenching. The binding constants of 3H-indole molecules with BSA were obtained. According to the Foerster resonance energy transfer theory, the distances between 3H-indole molecules and tryptophan of BSA were calculated. The results show that the oligoethyloxyethylene chain of 3H-indole molecules is longer, the binding between them is stronger, the energy transfer efficiency is higher, and the distance between tryptophan and 3H-indole is nearer.     

Conjugation of Chitooligosaccharide-5-fluorouracil with Bovine Serum Albumin

The interaction between chitooligosaccharide-5-fluorouracil (COS-5FU) and bovine serum albumin (BSA) was studied by fluorescence spectroscopy. It was found that an energy transfer between COS-5FU and BSA had been occurred. The binding constants were calculated, k298K=1.175×104 L·mol-1.Based on the mechanism of energy transfer of dipole-dipole interaction between the donor and acceptor, the distance between BSA and COS-5FU was determined.     

A Study on the Reaction Mechanism of Bromocresol Green with Bovine Serum Albumin

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Studies on Thermodynamics Features of the Interaction between Imidacloprid and Bovine Serum Albumin

At different temperatures, the interactions between imidacloprid （IMI） and bovine serum albumin （BSA） were investigated with a fluorescence quenching spectrum, a synchronous fluorescence spectrum, a three-dimensional fluorescence spectrum and an ultraviolet-visible spectrum. The average values of bonding constants （KLB： 3.424 × 10^4 L,mol^-1）, thermodynamic parameters （△H： 5.188 kJ,mol^-1, △G^（○—）：-26.36 kJ,mol^-1, △S： 103.9 J,K^-1,mol^-1） and the numbers of bonding sites （n： 1.156） could be obtained through Stern-Volmer, Lineweaver-Burk and ther- modynamic equations. It was shown that the fluorescence of BSA could be quenched for its reactions with IMI to form a certain kind of new compound. The quenching belonged to a static fluorescence quenching, with a non-radiation energy transfer happening within a single molecule. The thermodynamic parameters agree with △H〉 0, △S〉0 and△G^（○-）〈0, suggesting that the binding power between IMI and BSA should be mainly a hydrophobic interaction.     

Interaction Between Ranitidine Hydrochloride and Bovine Serum Albumin in Aqueous Solution

The interaction between ranitidine hydrochloride (RAN) and bovine serum albumin (BSA) in aqueous solution was investigated by means of fluorescence, synchronous fluorescence, and UV-Vis spectroscopy. The fluorescence of BSA was quenched remarkably by RAN and the quenching mechanism was concluded to be static quenching. The binding constants K and the number of binding sites n were calculated at three different temperatures. The RAN–BSA binding distance was determined to be less than 8 nm, suggesting that energy transfer may occur from BSA to RAN. The interaction process is spontaneous. Based on the obtained thermodynamic parameters, electrostatic forces may play a major role in this process. In addition, the effect of RAN on the conformation of BSA was analyzed using synchronous fluorescence spectra.     

Studies on Interaction between Gatifloxacin and Bovine Serum Albumin by Spectroscopy

The interaction of gatifloxacin （HGA） with bovine serum albumin （BSA） at 15 and 37 ℃ has been investigated by fluorescence quenching spectroscopy in aqueous solution. The bimolecular quenching rate constant was determined by Stem-Volmer curves and the values were Kq=9.28× 10^12 L·mol^-1·s^-1 （15 ℃） and Kq=8.51 ×10^12 L·mol^-1·s^-1 （37 ~C）. The results showed that the fluorescence quenching mechanism of BSA by HGA was a static quenching procedure. The thermodynamic parameters indicated that electrostatic forces played major role in the interaction of BSA with HGA. Studies on the relationship between the concentration of HGA and the fluorescence intensity of BSA showed that BSA and HGA bound at the molar ratio 1 ： 1 and the equilibrium constant K0 was 6.80 ×10^4 L·mol^-1. The binding distances between BSA and HGA and the energy transfer efficiency were obtained based on the Ftrster＇s theory.     

Interaction of Co（ll） with Bovine Serum Albumin under UV C Irradiation

The interaction of Co（Ⅱ） with BSA under UV C （253.7 nm） irradiation under physiological conditions has been studied by UV-vis spectrum, ultraviolet second-derivative spectroscopy and fluorescence spectrum. The quenching rate constant kq and the association constant Ka were calculated according to Stern-Volmer equation based on the quenching of the fluorescence of BSA by Co（Ⅱ）.     

Interaction between Glyoxal-bis-(2-hydroxyanil) and Bovine Serum Albumin in Solution

The interaction between glyoxal-bis-(2-hydroxyanil) (GBH) and bovine serum albumin (BSA) was studied by spectroscopic methods including fluorescence spectroscopy, circular dichroism (CD) and UV–visible absorption spectra. The mechanism for quenching the fluorescence of BSA by GBH is discussed. The number of binding sites n and observed binding constant K _b were measured by the fluorescence quenching method. The thermodynamic parameters ΔH ^θ , ΔG ^θ , and ΔS ^θ were calculated at different temperatures and the results indicate that hydrogen bonding and van der Waals forces played major roles in the reaction. The distance r between the donor (BSA) and acceptor (GBH) molecules was obtained according to Förster’s theory of non-radiation energy transfer. Synchronous fluorescence and three-dimensional fluorescence spectra were used to investigate the structural change of BSA molecules that occur upon addition of GBH, and these results indicate that the secondary structure of BSA molecules is changed by the presence of GBH.     

Interaction of Curculigosides and Their ��-Cyclodextrin Complexes with Bovine Serum Albumin: A Fluorescence Spectroscopic Study

Curculigosides A and B, two of the phyto-constituents of the medicinal plant Curculigo orchioides gatern, were isolated. The binding properties of these curculigosides with ??-cyclodextrin, and their interaction with bovine serum albumin in free and ??-cyclodextrin-complexed forms, were studied using fluorescence spectroscopy. The stoichiometry and binding constants of these complexes together with their binding modes are reported. Both of the curculigoside?Ccyclodextrin complexes are found to bind more weakly to the bovine serum albumin molecule than their free forms. The difference in the binding strengths of curculigoside A and curculigoside B with cyclodextrin makes a difference in their binding with bovine serum albumin.     

Design and Synthesis of 6 α-Corticosteroid Haptens and Their Bovine Serum Albumin(BSA) Conjugates

The site of attachment of protein carrier to corticosteroids has great influence on the specificity of produced antibody.In order to obtain highly specific and accurate antibodies for bioimmunoassay determination of cortisol,different tether lengths of 60633－corticosteroid haptens and their BSA conjugates were designed and synthesized.     

In Vitro Study of the Binding of Taxifolin to Bovine Serum Albumin and the Influence of Common Ions on the Binding

The interaction between taxifolin and bovine serum albumin (BSA), and the effects of some common ions on their interaction, were investigated by fluorescence and UV-visible absorption spectroscopy. The results indicate that taxifolin has a strong ability to quench the intrinsic fluorescence of BSA through a static quenching process. According to values of the thermodynamic parameters, the hydrophobic force plays a major role in the interaction. Based on Főster’s non-radiation theory, the energy transfer distances between BSA and taxifolin in the absence and presence of some common ions were obtained. The experimental results indicate that the transfer distances are almost unaffected by these ions. The conformation of BSA undergoes significant change from the formation of a taxifolin–BSA complex, which was studied by synchronous and three-dimensional fluorescence spectroscopy.     

Spectroscopic Study on the Interaction between Bovine Serum Albumin and Tween‐20

The interaction between nonionic surfactant Tween-20 and bovine serum albumin (BSA) is studied in Tris‐HCl buffer solution by spectroscopic methods. The intrinsic fluorescence of BSA is quenched by the addition of Tween‐20. The UV‐visible absorption spectra and the synchronous fluorescence spectra show that the addition of Tween‐20 changes the polarity of the environment around tryptophan (trp) residues of BSA. The fraction of trp residues on the surface of BSA with and without Tween- 20 is calculated via I^? quenching experiments.     

A Comparison Study on the Interaction of Sunset Yellow and β-Carotene with Bovine Serum Albumin

在模拟生理pH条件（pH=7．4）下,采用多种光谱法研究日落黄和β-胡萝卜素与BSA的相互作用,并比较两者与BSA相互作用过程的差异性．通过荧光光谱法和紫外吸收光谱法确定了日落黄和β-胡萝卜素对牛血清白蛋白的荧光猝灭机制,采用Stern—Volmer、双对数方程和热力学公式求出相互作用的猝灭常数、结合常数配、结合位点数月和作用力类型．结果表明：日落黄和β-胡萝卜素对BSA的猝灭属于静态猝灭,两者与BSA的民都达到10^5L／mol,结合位点数均为1,日落黄与BSA的作用力以静电引力为主,而β-胡萝卜素则是通过氢键和范德华力与BSA作用．通过红外光谱法和圆二色谱法研究了二者对BSA构象的影响,结果表明,日落黄与BSA作用的过程中,会引起BSA二级结构的改变,而β-胡萝卜素则对BSA的构象基本不产生影响．     

Investigation of the Interaction between Isoflavonoids and Bovine Serum Albumin by Fluorescence Spectroscopy

The interactions of bovine serum albumin （BSA） with three structurally related isoflavonoids, genistein, puerarin and daidzein, were studied under physiological conditions by fluorescence spectroscopic technique. The quenching mechanism of these compounds with BSA was suggested as static quenching and the binding constants were determined at different temperatures based on the fluorescence quenching results. The transfer efficiency of energy and distance between the acceptor and BSA were investigated on the basis of the mechanism of the Forster energy transference. According to the thermodynamic parameters it has been suggested that the acting force be mainly hydrophobic force. The comparison of binding potency of the three isoflavonoids to BSA showed that the substitution by 5-OH and 8-Glc could enhance the binding affinity. All these obtained in the work can make us better understand the mode of the action and pharmacological activities of the isoflavonoids.     

A Study on the Interaction of the DAS-K with Bovine Serum Albumin by On-line Ultrafiltration and Chemiluminescence

Potassium dehydroandrographolide succinate （DAS-K） has antibacterial and antiviral effects. It has been used widely for the treatment of virus pneumonia, malaria and respiratory infections. In this work, a novel flow-injection chemiluminescence （CL） method for the determination of DAS-K was proposed. The method is based on the reaction between DAS-K and hexacyanoferrate（III） in alkaline solution to give weak CL signal, which is enhanced by rhodamine B. The experimental conditions for the CL reaction were optimized and the possible reaction mechanism was discussed. Under the optimum conditions, the concentration of DAS-K is proportional to the CL intensity in the range of 0.1-80 μmol·L^-1 with a detection limit of 0.05 μmol·L^-1. The interaction of the DAS-K with bovine serum albumin by on-line ultrafiltration and flow-injection chemiluminescence was studied. The concentrations of unbound DAS-K from ultra filter tube were determined by the flow-injection CL method. The binding parameters were estimated by the Scatchard plot and Klotz plot. The proposed system proved that FIA-CL coupled with on-line ultrafiltration sampling was a fast and simple technique for the study of drug-protein interaction.     

Association Constants in the Bovine Serum Albumin/Human Serum Albumin–Tween 20 System in Aqueous Solutions

The association constants in the bovine serum albumin/human serum albumin–Tween 20 system are determined in aqueous solutions at pH 3.5–8.0 by means of nonpolarized fluorescence and protein fluorescence quenching. It is found that the most efficient association of serum albumin molecules with Tween 20 micelles occurs at pH 5.0 near the isoelectric points of proteins.     

Study on the Interaction between Strychnine and Bovine Serum Albumin by Capillary Electrophoretic Frontal Analysis

Most drugs are usually bound to proteins such as serum albumin,α1-acid glycoprotein,lipoprotein,and other blood constituents.The plasma concentration of an unbound drug shows better correlation to the pharmaceutical activity1.It is therefore necessary to know the extent of drug-protein binding in order to adjust the optimal therapeutic dose of the drug.Strychnos nux-vomica L.(Loganiaceae)is an evergreen tree native to southeast Asia.Its dried seeds are used for treatment of nervous diseases…     

Characterization of the Interaction between Bovine Serum Albumin and Lomefloxacin by Capillary Zone Electrophoresis

Three capillary zone electrophoresis (CZE) methods of the frontal analysis (FA), vacancypeak (VP) and simplified Hummel-Dreyer (SHD) were applied to investigate interaction betweenbovine serum albumin (BSA) and lomefloxacin, the experimental condition was established after alarge number of tests. Based on the site-binding model, the binding parameters were measuredaccording to the site model by Scatchard.