Study on the interaction of bovine serum albumin with acid cyanine 5R and its application in analysis

2006 ◽  
Vol 84 (1) ◽  
pp. 1-8 ◽  
Author(s):  
Fei Lu ◽  
Jing-Hao Pan ◽  
Yun Liu ◽  
Hongfen Zhang ◽  
Yujing Guo ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Binding Constant ◽  
Bovine Serum ◽  
Peak Potential ◽  
Buffer Solution ◽  
Solution Ph ◽  
Peak Current ◽  
Binding Ratio ◽  
Relative Standard

A supramolecular complex of bovine serum albumin (BSA) with acid cyanine 5R (AC 5R, C.I. acid blue 113, C.I.: 26360) has been shown to form in Tris–HCl buffer solution (pH 7.42) by linear sweep voltammetry (LSV), fluorimetry, and spectrophotometry. The binding ratio and binding constant of BSA with AC 5R have been detected by LSV and fluorimetry. The binding mechanism is also preliminarily discussed. In Tris–HCl buffer solution (pH 7.42), AC 5R can easily be reduced on the mercury electrode, and it has a well-defined LSV peak current (Ip) and peak potential (Ep) at –0.65 V (vs. SCE). In the presence of BSA, the Ipof AC 5R decreases, and the peak potential (Ep) shifts to a more positive potential. The decrease of the second-order derivative of reductive peak current (ΔIp") of AC 5R is proportional to the logarithm of BSA concentration in the range of 1.54 × 10–8mol·L–1– 1.54 × 10–5mol·L–1(r = 0.9931 – 0.9977). The limit of detection of BSA is 9.0 × 10–9mol·L–1. The relative standard deviation is 1.83% (n = 10), and the standard recovery is 97.5%–104.8%. This method can be used to determine BSA concentration on the basis of the interaction of BSA with AC 5R.Key words: bovine serum albumin (BSA), acid cyanine 5R (AC 5R), supramolecule, binding ratio, binding constant, fluorimetry, spectrophotometry, electroanalytical method.

Phosphotungstic Acid, Silicotungstic Acid and Silicon Tungsten-Cobalt Heteropoly Acid with Bovine Serum Albumin Interaction

2013 ◽  
Vol 652-654 ◽  
pp. 722-725
Author(s):  
Wei Yang Shen ◽  
Min Xin Song ◽  
Jian Qiu Chen ◽  
Rui Xin Guo
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Heteropoly Acid ◽  
Phosphotungstic Acid ◽  
Silicotungstic Acid ◽  
Buffer Solution ◽  
Solution Ph ◽  
Uv Absorption Spectroscopy ◽  
Tris Buffer Solution

The interactions of bovine serum albumin (BSA) with phosphotungstic heteropoly acid (PW), silicon tungsten heteropoly acid (SiW) and silicon tungsten-cobalt acid (SiWCo) were studied by fluorescence spectroscopy and UV absorption spectroscopy at Tris buffer solution (pH = 7.40). It was found that the fluorescence quenching of PW, SiW and SiWCo with BSA was static and the binding constant, binding site and the thermodynamic parameters were calculated at 298 and 310K. In addition, the conformations of BSA impacted by PW, SiW and SiWCo were researched using synchronous fluorescence. The results showed that PW, SiW and SiWCo all could interact with BSA but they had not changed the conformation of BSA.

A Novel Conjugated Polyfluorene: Synthesis, Characterization and Application in Flow Injection Electrochemiluminescence for Detection of Bovine Serum Albumin

2013 ◽  
Vol 575-576 ◽  
pp. 107-110
Author(s):  
Shu Ai Li ◽  
Shao Wei Wang ◽  
Cheng Chao Chu ◽  
Xiu Wang ◽  
Mei Yan ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Water Soluble ◽  
Applied Potential ◽  
Visible Spectroscopy ◽  
Buffer Solution ◽  
Solution Ph ◽  
Strong Fluorescence ◽  
Phosphate Buffered Saline

Driven by the urgent demand for novel electrochemiluminescence reagents, a water-soluble polyfluorene derivative, poly [(9,9-bis (3-((N,N-dimethylamino)N-ethy-lammonium) propyl)-2,7-fluorene)-alt-2,7-(9,9-p-divinylbenzene)] dibromide (P-2), was designed and success-fully synthesized. Ultraviolet-visible spectroscopy and fluorescence spectroscopy were used to characterize the formation of P-2, and the results showed that P-2 had strong fluorescence intensity. More importantly, electrochemiluminescence (ECL) of the prepared P-2 was also observed when the applied potential was cycled between 1.0 to 2.8 V at 100 mV·s-1 in phosphate buffered saline buffer solution (pH 8.20). Based on the stable ECL performance, an ECL system for bovine serum albumin (BSA) was constructed. Under the optimal conditions, the enhanced ECL intensity was linearly correlated to the concentration of BSA over the range of 5.0×10-8-1×10-4 g·mL-1 (R=0.9996) with a detection limit of 1.26×10-8 g·mL-1 (n=11). This work not only introduced a substitute for traditional ECL regents, but also proposed a simple ECL system for other analytes.

Bioceramic Hydroxyapatite Granules for Purification of Biotechnological Products

2011 ◽  
Vol 284-286 ◽  
pp. 1764-1769 ◽  
Author(s):  
Vitalijs Lakevics ◽  
Janis Locs ◽  
Dagnija Loca ◽  
Valentina Stepanova ◽  
Liga Berzina-Cimdina ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Phosphate Buffer ◽  
Bovine Serum ◽  
Phosphate Buffer Solution ◽  
Sorption Process ◽  
Buffer Solution ◽  
Ph Values ◽  
Bovine Serum Albumin Adsorption ◽  
Albumin Adsorption

Sorption experiments of bovine serum albumin (BSA) on hydroxyapatite (HAp) ceramic granules, prepared at three temperatures 900°C, 1000°C and 1150°C were performed at room temperature 18,6 °C and phosphate buffer, pH 5,83; 6.38 and 7,39. Thermal treatment contributed to the decrease of bovine serum albumin immobilization indicating that sorption process depended on HAp ceramics specific surface area and pH values of phosphate buffer solution. However, it was confirmed that granule size was also an important parameter for bovine serum albumin adsorption. As a result of these experiments, the most appropriate adsorption conditions and phosphate buffer pH values influence on to BSA sorption were analyzed.

Langmuir Aggregation of Eosin-Y in Protein and its Application

2002 ◽  
Vol 55 (12) ◽  
pp. 767 ◽  
Author(s):  
Hong-Wen Gao ◽  
Jian-Fu Zhao
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Concanavalin A ◽  
Bovine Serum ◽  
Quantitative Detection ◽  
Eosin Y ◽  
Isothermal Adsorption ◽  
Adsorption Reaction ◽  
Binding Ratio ◽  
Langmuir Aggregation

The microsurface adsorption–spectral correction (MSASC) technique is described and applied to the investigation of the interaction of eosin-Y (EOY) with proteins at pH 3.8. The microelectrostatic fields in proteins cause the aggregation of EOY and it obeys Langmuir isothermal adsorption. Results have shown that the binding ratio of EOY to bovine serum albumin (BSA), ovalbumin (OVA), concanavalin A (ConA), and human γ-globulin (γ-G) are 77 : 1, 23 : 1, 4 : 1, and 83 : 1, the adsorption constants of the complexes were calculated to be 2.82×106, 1.70×105, 1.80×105, and 2.49×104 M–1, and their molar absorptivities 3.20×106, 1.21×106, 1.35×105, and 5.27×106 L mol–1 cm–1 at 540�nm. The adsorption reaction has been applied to the quantitative detection of proteins in samples with satisfactory results.

scholarly journals Formation and Stabilization of Gold Nanoparticles in Bovine Serum Albumin Solution

Molecules ◽  
2019 ◽  
Vol 24 (18) ◽  
pp. 3395 ◽  
Author(s):  
Iulia Matei ◽  
Cristina Maria Buta ◽  
Ioana Maria Turcu ◽  
Daniela Culita ◽  
Cornel Munteanu ◽  
...  
Keyword(s):  
Gold Nanoparticles ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Particle Growth ◽  
Protective Role ◽  
Amino Acid Residues ◽  
Buffer Solution ◽  
Paramagnetic Resonance ◽  
Tem Microscopy

The formation and growth of gold nanoparticles (AuNPs) were investigated in pH 7 buffer solution of bovine serum albumin (BSA) at room temperature. The processes were monitored by UV-Vis, circular dichroism, Raman and electron paramagnetic resonance (EPR) spectroscopies. TEM microscopy and dynamic light scattering (DLS) measurements were used to evidence changes in particle size during nanoparticle formation and growth. The formation of AuNPs at pH 7 in the absence of BSA was not observed, which proves that the albumin is involved in the first step of Au(III) reduction. Changes in the EPR spectral features of two spin probes, CAT16 and DIS3, with affinity for BSA and AuNPs, respectively, allowed us to monitor the particle growth and to demonstrate the protective role of BSA for AuNPs. The size of AuNPs formed in BSA solution increases slowly with time, resulting in nanoparticles of different morphologies, as revealed by TEM. Raman spectra of BSA indicate the interaction of albumin with AuNPs through sulfur-containing amino acid residues. This study shows that albumins act as both reducing agents and protective corona of AuNPs.

The Study on the Interaction Conditions of Water-Soluble Chitosan with Bovine Serum Albumin

2011 ◽  
Vol 347-353 ◽  
pp. 1281-1286
Author(s):  
Shan Shan Huang ◽  
Feng Zuo Qu ◽  
Tong Kuan Xu ◽  
Li Cui
Keyword(s):  
Bovine Serum Albumin ◽  
Fluorescence Quenching ◽  
Serum Albumin ◽  
Linear Relationship ◽  
Binding Constant ◽  
Bovine Serum ◽  
Fluorescence Spectra ◽  
Three Dimensional ◽  
Water Soluble ◽  
Visible Absorption

The interaction conditions between the water-soluble chitosans(WSC) and bovine serum albumin (BSA) was studied by Ultraviolet-visible absorption and fluorescence spectrometries. It was shown there was a good linear relationship between the absorbency A and the BSA concentration(0~1.5g/L) and WSC concentration (0~1.5 g/L). The fluorescence quenching of WSC to BSA was static quenching. When the temperature is 30°C, its binding constant Ka=5.35×104 L/mol, binding site n=1.05. The influence of WSC on the conformation of BSA was analyzed by sychronous fluorescence spectra and three-dimensional fluorescence spectrum.

The Effect of Bovine Serum Albumin on the Binding Constant and Stoichiometry of Biocompatible Magnetic Fluids

2004 ◽  
Vol 40 (4) ◽  
pp. 3027-3029 ◽  
Author(s):  
P.P. Macaroff ◽  
D.M. Oliveira ◽  
Z.G.M. Lacava ◽  
R.B. Azevedo ◽  
E.C.D. Lima ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Binding Constant ◽  
Bovine Serum ◽  
Magnetic Fluids

scholarly journals The Bovine Serum Albumin Coated Copper Oxide Nanoparticle for Curcumin Delivery in Biological Environment: In-vitro Drug Release

2021 ◽  
Author(s):  
Tahmineh Atloo ◽  
Ramin Mohammadkhani ◽  
Ali Mohammadi ◽  
Kasra Arbabi Zaboli ◽  
Saeed Kaboli ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Drug Release ◽  
Serum Albumin ◽  
Copper Oxide ◽  
Cell Line ◽  
Bovine Serum ◽  
Copper Oxide Nanoparticles ◽  
Buffer Solution ◽  
Biological Environment

Abstract In this work, first, copper oxide nanoparticles (CUO NPs) were synthesized by physical methods and then coated with the bovine serum albumin (BSA) via biologically meditated minerals to form CUO@BSA NPs. Finally, curcumin (CUR) as an anticancer drug were immobilized on the surface of CUO@BSA NPS. The properties of CUO@BSA-CUR NPS were investigated by FTIR, UV-Vis, TEM, and AFM spectroscopes. It was found that the synthesized CUO@BSA-CUR nanoparticles were spherical with a particle size of 20 to 30 nm and have a sustained release of CUR at 37°C in buffer solution. Also, the result of release in biological environment showed that maximum drug release rate for this nanocarrier in pH 7.4 was measured 75% after 48 hours. The cytotoxicity of CUO@BSA-CUR on MDA-MB-231 cell line was studied. The results showed that CUO@BSA-CUR nanoparticles have significant cytotoxic activity on this cell line, while the results of MTT assay indicated the CUO@BSA NPs have no toxicity effect on the cancer cells.

Hyperosmotic Infiltration: Factors Influencing Uptake of Bovine Serum Albumin by Rainbow Trout (Salmo gairdneri)

1978 ◽  
Vol 35 (6) ◽  
pp. 871-874 ◽  
Author(s):  
D. C. Fender ◽  
D. F. Amend
Keyword(s):  
Rainbow Trout ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Osmotic Pressure ◽  
Bovine Serum ◽  
Immersion Time ◽  
Salmo Gairdneri ◽  
Nacl Solution ◽  
Step Method ◽  
Solution Ph

Infiltration of bovine serum albumin (BSA) into the blood of rainbow trout (Salmo gairdneri) by hyperosmotic infiltration (HI) was studied by varying the osmotic pressure, immersion time, pH, temperature, stress, vacuum, and fish size. Compared with uptake of BSA from water solutions, about 1400 mosM (4.51%) NaCl was required to increase the plasma level of BSA during a 3-min immersion. Higher osmotic pressures resulted in higher plasma-BSA levels, but the uptake of BSA was limited by the length of time that fish could tolerate the high NaCl concentration. Comparison of immersion time in the solutions of the two-step HI method showed that maximum infiltration occurred after a 2–3-min bath in the 5.32% NaCl solution and only 30 s in the 2% BSA solution. Alkaline solution (pH 9) enhanced BSA uptake in the one-step method, but the two-step method was most effective if the NaCl solution was pH 9 and the BSA solution pH 5. BSA uptake was directly proportional to water temperature from 4 to 20 °C. Preimmersion stress, and injection of 10 μg epinephrine, reduced BSA uptake; vacuum and fish weight (2–8 g) had no effect on uptake of BSA. Hyperosmotic infiltration may be useful for mass delivery of vaccines, pharmaceuticals, and other materials. Key words: hyperosmotic infiltration, bovine serum albumin, osmotic pressure, vaccines, immersion, rocket immunoelectrophoresis

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