Interaction Between Gatifloxacin and Bovine Serum Albumin

Aim To study the reaction mechanism between gatifloxacin and bovine serumalbumin (BSA) at different pHs. Methods Fluorescence spectra and UV absorbance spectra were used.Results The binding constants were determined from a double reciprocal Lineweaver-Burk curves atdifferent pHs. The binding distance r under normal physiological condition was obtained according toFoster theory of non-radiative energy transfer. The binding force between gatifloxacin and BSA wasinferred by thermody-namical coordination. Conclusion The interaction between gatifloxacin and BSAseems to be strong and the main binding force is electrostatic force.

(E)-2-Benzylidenecycloalkanones XII.*Kinetic Measurement of Bovine and Human Serum Albumine Interaction with Selected Chalcones and Their Cyclic Chalcone Analogues by UV Spectrophotometry

UV-VIS spectroscopic investigations of interaction of bovine and human serum albumin with selected chalcones (1) and their cyclic chalcone analogues: (E)-2-(4’-X-benzylidene-1-tetralones (3), benzosuberones (4) with dimethylamino and methoxy substituents and (E)-2-(2’,4’-dimethox- ybenzylidene)-1-indanone (2) were performed in polar respiration medium. Absorption maxima of the tested compounds were investigated in the presence of bovine and human serum albumin at the 0, 10, 30 and 60 minute timepoints of the interaction. The absorbance of all studied compounds in the presence of proteins decreased after one hour of the reaction. Molecule 4a showed the strongest and fastest kinet initial interaction with both albumins.

Spectroscopic analysis on the binding interaction of biologically active pyrimidine derivative with bovine serum albumin

A biologically active antibacterial reagent, 2-amino-6-hydroxy-4-（4-N, N-dimethylaminophenyl）-pyr- imidine-5-carbonitrile （AHDMAPPC）, was synthesized. It was employed to investigate the binding in- teraction with the bovine serum albumin （BSA） in detail using different spectroscopic methods. It ex- hibited antibacterial activity against Escherichia cali and Staphylococcus aureus which are common food poisoning bacteria. The experimental results showed that the fluorescence quenching of model carrier protein BSA by AHDMAPPC was due to static quenching. The site binding constants and number of binding sites （n ≈ 1） were determined at three different temperatures based on fluorescence quenching results. The thermodynamic parameters, enthalpy change （AH）, free energy （AG） and entropy change （AS） for the reaction were calculated to be 15.15 kJ/mol, -36.11 kJ/mol and 51.26J/mol K according to van＇t Hoff equation, respectively. The results indicated that the reaction was an endothermic and spontaneous process, and hydrophobic interactions played a major role in the binding between drug and BSA. The distance between donor and acceptor is 2.79 nm according to Forster＇s theory. The alterations of the BSA secondary structure in the presence of AHDMAPPC were confirmed by UV-visible, synchronous fluorescence, circular dichroism （CD） and three-dimensional fluorescence spectra. All these results in- dicated that AHDMAPPC can bind to BSA and be effectively transported and eliminated in the body. It can be a useful guideline for further drug design.

Immobilization of Bovine Serum Albumin on Poly(ether ether ketone) for Surface Biocompatibility Improvement

UV-induced graft polymerization of acrylic acid（AA） on poly（ether ether ketone）（PEEK） films was carried out to introduce ―COOH for the subsequent immobilization of bovine serum albumin（BSA）.BSA was introduced on PEEK surface based on the condensation reaction between ―NH 2 and ―COOH.The modified surface（PEEK-BSA） was characterized by energy-disperse spectrometry（EDS）,X-ray photoelectron spectroscopy（XPS）,water contact angle measurement and UV spectrum analysis.The contact angle was found to decrease from 104° for the virgin PEEK films to 63° for the BSA-immobilized PEEK films,demonstrating a significant improvement of surface hydrophilicity.Moreover,the appearance of nitrogen on PEEK film confirmed by XPS and EDS indicates the immobilization of BSA on PEEK surface.

Synthesis of Metal Porphyrins Tailed with Salicylic Acid and their Interaction with Bovine Serum Albumin

A synthetic method of porphyrins tailed with salicylic substituents is described. Reaction of bromoalkoxyphenyl porphyrin 1 with salicylic acid gave porphyrins 2~5. These new compounds were confirmed by 1H NMR, IR, UV-vis, MS and elemental analysis, and observed their interaction with bovine serum albumin (BSA) in fluorescence spectrum.

Sonocatalytic Damage of Bovine Serum Albumin (BSA) in the Presence of Nanometer Titanium Dioxide (TiO_2) Catalyst

The sonocatalytic damage of bovine serum albumin （BSA） was studied in the presence of nanometer titanium dioxide （TiO2） powders by low frequency （80 kHz） ultrasound. The destruction of secondary structure and change of α-helical structure of BSA were reflected by ultraviolet （UV） and circular dichroism （CD） spectroscopies.

Dynamic Behaviors and Morphology Change of Anionic Phospholipid DPPG Monolayer Caused by Bovine Serum Albumin at Air-Water Interface

The interaction between bovine serum albumin （BSA） and the anionic 1.2-dipalmitoyl-snglycero- 3-（phospho-rac-（1-glycerol）） （sodium salt） （DPPG） phospholipid at different subphase pH values was investigated at air-water interface through surface pressure measurements and atomic force microscopy （AFM） observation. By analyzing surface pressure-mean molecular area （π-A） isotherms, the limiting molecular area in the closed packing state-the concentration of BSA （Alim-[BSA]） curves, the compressibility coefficient-surface pressure （CS-1-π） curves and the difference value of mean molecular area-the concentration of BSA （ΔA-[BSA]） curves, we obtained that the mean molecular area of DPPG monolayer became much larger when the concentration of BSA in the subphase increased at pH=3 and 5. But the isotherms had no significant change at different amount of BSA at pH=10. In addition, the amount of BSA molecules adsorbed onto the lipid monolayer reached a threshold value when [BSA]〉5×10-8 mol/L for all pHs. From the surface pressure-time （π-t） data, we obtained that desorption and adsorption processes occurred at pH=3, however, there was only desorption process occurring at pH=5 and 10. These results showed that the interaction mechanism between DPPG and BSA molecules was affected by the pH of subphase. BSA molecules were adsorbed onto the DPPG monolayers mainly through the hydrophobic interaction at pH=3 and 5, and the strength of hydrophobic interaction at pH=3 was stronger than the case of pH=5. At pH=10, a weaker hydrophobic interaction and a stronger electrostatic repulsion existed between DPPG and BSA molecules. AFM images revealed that the pH of subphase and [BSA] could affect the morphology features of the monolayers, which was consistent with these curves. The study provides an important experimental basis and theoretical support to understand the interaction between lipid and BSA at the air-water interface.

Determination of Enantiomeric Compositions of Tryptophan by Chemometric Analysis of the Fluorescence Spectra of Bovine Serum Albumin Receptor-ligand Mixtures

In this work, a novel method was constructed to determine the enantiomeric composition of tryptophan （Trp） by bovine serum albumin （BSA） based on the fluorescence spectra of the receptor-ligand mixtures coupled with partial least squares （PLS-1） analysis. As a result the enantiomeric composition of Trp was accurately determined.

Antioxidant activity of bovine serum albumin binding amino acid Schiff-bases metal complexes

Glutamic acid-salicylaldehyde Schiff-base metal complexes are bound into bovine serum albumin （BSA）, which afforded BSA binding Schiff-base metal complexes （BSA-SalGluM, M=Cu, Co, Ni, Zn）. The BSA binding metal complexes were characterized by UV-vis spectra and Native PAGE. It showed that the protein structures of BSA kept after coordinating amino acid Schiff-bases metal complexes. The effect of the antioxidant activity was investigated. The results indicate that the antioxidant capacity of BSA increased more than 10 times after binding Schiff-base metal complexes.

Using capillary electrophoresis mobility shift assay to study the interaction of CdTe quantum dots with bovine serum albumin

In this work, the capillary electrophoresis mobility shift assay （CEMSA） was first adopted to study the interaction of protein with quantum dots （QDs）. In this study, bovine serum albumin （BSA） and CdTe QDs were used as model samples. We observed that BSA was facilely adsorbed to CdTe QDs surface, and the QD-BSA complex was formed by a 1：1 stoichiometric ratio. A value of 2.17 4-0.27 × 10^6 mol^-1 L^-1 （at 25 ℃） for the association constant was obtained by CEMSA.

Characterization of Interaction Between Raltitrexed and Bovine Serum Albumin by Optical Spectroscopic Techniques

The interaction of raltitrexed（RTX） with bovine serum albumin（BSA） was investigated by steady state/lifetime fluorescence spectroscopy and circular dichroism（CD） spectroscopy under the simulative physiological conditions.The results of fluorescence titration reveal that RTX could strongly quench the intrinsic fluorescence of BSA via a static quenching procedure.The obtained binding constant K A of RTX with BSA was 478630 and 44259 L/mol at 298 and 310 K,respectively.According to van＇t Hoff equation,the thermodynamic parameters ΔH,ΔG and ΔS were calculated,indicating that hydrophobic forces were the predominant intermolecular forces in stabilizing the complex.The binding process was a spontaneous process,in which Gibbs free energy change was negative.According to F rster＇s non-radioactive energy transfer theory,the distance r between donor（BSA） and acceptor（RTX） was 3.82 nm,suggesting that the energy transfer from BSA to RTX occurred with high probability.Displacement experiment and the number of binding sites calculation confirmed that RTX could bind to the site-I of BSA.Furthermore,the effects of pH and some metal ions on the interaction of RTX with BSA were also investigated.The results of synchronous fluorescence and CD spectra show that the RTX-BSA binding induced conformational changes in BSA.

Binding interactions of pefloxacin mesylate with bovine lactoferrin and human serum albumin

The binding of pefloxacin mesylate （PFLX） to bovine lactoferrin （BLf） and human serum albumin （HSA） in dilute aqueous solution was studied using fluorescence spectra and absorbance spectra. The binding constant K and the binding sites n were obtained by fluorescence quenching method. The binding distance r and energy-transfer efficiency E between pefloxacin mesylate and bovine lactoferrin as well as human serum albumin were also obtained according to the mechanism of Forster-type dipole-dipole nonradiative energy-transfer. The effects of pefloxacin mesylate on the conformations of bovine lactoferrin and human serum albumin were also analyzed using synchronous fluorescence spectroscopy.

Morphological characterization of metal porphyrin tailed with aspirin interacting with bovine serum albumin congeries

The porphyrins tailed with acetylsalicylic acid （ASA） and Zn （or Cu） complexes were prepared. Meanwhile, morphological images, such as shape and size of porphyrins-BSA congeries were observed by using atomic force microscopy （AFM）. The result showed the interaction of BSA and prepared porphyrins led to obvious change of shape and size of BSA congeries.

Effects of urea,metal ions and surfactants on the binding of baicalein with bovine serum albumin

The interaction of baicalein with bovine serum albumin（BSA） was investigated with the help of spectroscopic and molecular docking studies.The binding affinity of baicalein towards BSA was estimated to be in order of 10~5 M^（-1） from fluorescence quenching studies.Negative ΔH°（-5.66 ＋ 0.14 kJ/mol） and positive（ΔS°）（＋ 79.96 ＋ 0.65J/mol K） indicate the presence of electrostatic interactions along with the hydrophobic forces that result in a positive ΔS°.The hydrophobic association of baicalein with BSA diminishes in the presence of sodium dodecyl sulfate（SDS） due to probable hydrophobic association of baicalein with SDS,resulting in a negative ΔS°（-40.65 ＋ 0.87 J/mol K）.Matrix-assisted laser desorption ionization/time of flight（MALDI-TOF） experiments indicate a 1：1 complexation between baicalein and BSA.The unfolding and refolding phenomena of BSA were investigated in the absence and presence of baicalein using steady-state and fluorescence lifetime measurements.It was observed that the presence of urea ruptured the non-covalent interaction between baicalein and BSA.The presence of metal ions（Ag~＋,Mg^（2＋）,Ni^（2＋）,Mn^（2＋）,Co^（2＋） and Zn^（2＋）） increased the binding affinity of ligand towards BSA.The changes in conformational aspects of BSA after ligand binding were also investigated using circular dichroism（CD） and Fourier transform infrared（FT-IR） spectroscopic techniques.Site selectivity studies following molecular docking analyses indicated the binding of baicalein to site 1（subdomain MA） of BSA.

Bovine serum albumin:An efficient and green biocatalyst for the one-pot four-component synthesis of pyrano[2,3-c]pyrazoles

The use of biocatalysts is attracting an increasing amount of attention in chemical catalysis.Here,we have shown that bovine serum albumin（BSA）,a ubiquitous,inexpensive,non-enzymatic transport protein,can serve as an efficient,retrievable catalyst in the one-pot four-component reaction of aryl aldehydes,malononitrile,hydrazine hydrate,and ethyl acetoacetate for the synthesis of pyrano[2,3-c]pyrazoles under mild reaction conditions.The BSA biocatalyst also displayed a high catalytic affinity for acyclic/cyclic ketones to yield the corresponding pyrano[2,3-c]pyrazoles or their spirocyclic variants.The BSA could be used for at least five cycles without serious loss of catalytic activity.This novel,efficient protocol has the merits of high yield,operational simplicity,and a relatively benign environmental impact.Moreover,the method extends the promiscuity of BSA as a biocatalyst.

Synthesis of Zinc Oxide Nanoparticles with Good Photocatalytic Activities under Stabilization of Bovine Serum Albumin

Zinc oxide nanoparticles were synthesized using bovine serum albumin as stabilizers through a facile one-pot strategy in aqueous media. The morphology and crystal phase of the zinc oxide nanoparticles were determined by transmission electron microscopy, X-ray diffractograms, and Fourier transform infrared spectroscopy. The synthesized ZnO nanoparticles exhibited strong absorption and photoluminescence properties in the visible wavelength region based on the fluorescence and UV-visible spectroscopy. Based on the results, the zinc oxide nanoparticles could effectively degrade the organic dyes through the mediation of the hydroxyl radical under visible light irradiation. Furthermore, the zinc oxide nanoparticles show good recycling stability during the photocatalytic experiments. These results suggested that the as-prepared zinc oxide nanoparticles might be used as a potential photocatalyst to efficiently treat the organic pollutants.

Reduced graphene oxide-grafted bovine serum albumin/bredigite nanocomposites with high mechanical properties and excellent osteogenic bioactivity for bone tissue engineering

The optimization of the scaffolds to provide a suitable matrix and accelerate the regeneration process is vital for bone tissue engineering.However,poor mechanical and biological characteristics remain the primary challenges that must be addressed.For example,although bredigite(Br)has shown great potential for application in bone tissue engineering,it easily fails in replacement.In the present work,these challenges are addressed by reinforcing the Br matrix with nanosheets of graphene oxide(rGO)that have been reduced by bovine serum albumin(BSA)in order to enhance the mechanical properties and biological behavior.The reduction of graphene oxide by BSA improves the water stability of the nanosheets and provides an electrostatic interaction between theBSA-rGO nanosheets and theBr particles.The high thermal conductivity of theBSA-rGO nanosheets decreases the porosity of the Br by transferring heat to the core of the tablet.Furthermore,the addition of BSA-rGO nanosheets into the Br matrix enhances the adhesion of G-292 cells on the surface of the tablets.These findings suggest that the tablet consisting of BSA-rGO-reinforced Br has encouraging potential for application in bone tissue engineering.

Microwave Synthesis of CdTe/TGA Quantum Dots and Their Thermodynamic Interaction with Bovine Serum Albumin

The thioglycollic acid（TGA） as a capping agent, CdTe/TGA quantum dots（QDs） with excellent properties were synthesized under microwave irradiation. The TGA/Cd/Te molar ratios, reaction time, temperature and p H are the crucial factors for properties of QDs. The QDs were characterized by UVvis absorption and fluorescence spectra, transmission electron microscopy and Fourier transform infrared spectroscopy. The experimental results show that when the p H value is 11.5 and molar ratio of TGA：Cd：Te is 1.2：1：0.4 at 100 ℃ heating for 15 min, the resulted QDs exhibit a high fluorescence quantum yield of 78%. The fluorescence full width at half maximum（FHMW） of QDs is around 23 nm. The products are spherical with average size of 3-5 nm. There is a strong coordination effect between TGA and Cd2＋. Moreover, the results of interaction between as-made QDs and bovine serum albumin（BSA） suggest that the QDs-BSA binding reaction is a static quenching. The negative values of free energy（△G〈0） suggest that the binding process is spontaneous, △H〈0 and △S〈0 show that hydrogen bonds and van der Waals interactions play a major role in the binding reaction between QDs and BSA.

Study on the interaction between clarithromycin and bovine serum albumin in the imitated physiology solution

The interaction between clarithromycin (CAM) and bovine serum albumin (BSA) was investigated using linear-sweep voltammetry in pH 7.4 phosphate buffer solution where CAM caused two irreversible reduction waves P2 and P3 on mercury electrode. The study showed that the formation constant and formation ratio for the interaction between CAM and BSA were 1.51 × 10(12) and 3:1 for P2, 4.53 × 10(5) and 1:1 for P3, respectively. The ion strength enhanced the hydrophobic interaction between CAM and BSA.

Study on the Interaction between CdSe Quantum Dots and Bovine Serum Albumin with Ultraviolet Visible Absorption Spectroscopy

The interaction of CdSe quantum dots （QDs） with bovine serum albumin （BSA） has been investigated with ultraviolet visible absorption spectroscopy （UVAS）. It was found that the absorption intensity of CdSe QDs significantly decreased after adding BSA solution, showing that CdSe QDs were bonded to BSA. The binding molar ratio was 1：1 and the binding constant was 9.7 × 10^6 L mol^-1.