scholarly journals Preparation and Characterization of Au/NiPc/Anti-p53/BSA Electrode for Application as a p53 Antigen Sensor

Chemosensors ◽  
2021 ◽  
Vol 9 (1) ◽  
pp. 17
Author(s):  
Yen-Jou Chen ◽  
Yu-Ren Peng ◽  
Hung-Yu Lin ◽  
Tsung-Yu Hsueh ◽  
Chao-Sung Lai ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Cell Damage ◽  
P53 Protein ◽  
Specific Antigen ◽  
P53 Gene ◽  
Buffer Solution ◽  
Detection Range ◽  
P53 Antibodies

While the tumor suppressor protein p53 regulates the cell cycle to prevent cell damage, it also triggers apoptosis and prevents cancer. These inhibitory functions may disappear once the p53 gene is mutated. Under these circumstances, the detection of p53 protein concentrations can have significant clinical applications. In this study, nickel phthalocyanine (NiPc) was coated on a gold electrode to produce a modified Au/NiPc electrode. p53 antibodies were bonded to the Au/NiPc electrode by the Ni+2 ion in NiPc, which can be self-assembled with the imidazole group of the p53 protein. The Au/NiPc/anti-p53 electrode was subsequently dripped with a buffer solution of bovine serum albumin (BSA) to form the Au/NiPc/anti-p53/BSA electrode, which was used for the detection of p53 antigen under 10 mM potassium ferricyanide/potassium ferrocyanide (K3Fe(CN)6/K4Fe(CN)6) solution by cyclic voltammetry and differential pulse voltammetry analyses. The linear detection range and the sensitivity for the p53 antigen were 0.1–500 pg/mL and 60.65 μA/Log (pg/mL)-cm2, respectively, with a detection time of 90–150 s. In addition, Au/NiPc/anti-p53 (100 ng/mL)/BSA electrodes were tested for specificity using glucose, bovine serum albumin, histidine, ascorbic acid, uric acid, prostate-specific antigen, human serum albumin, and human immunoglobulin G. All p-values were <0.0005, indicating an outstanding specificity.

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.

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.

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.

scholarly journals Influence of Bovine Serum Albumin (BSA) on the Tribocorrosion Behaviour of a Low Carbon CoCrMo Alloy in Simulated Body Fluids

Lubricants ◽  
2020 ◽  
Vol 8 (5) ◽  
pp. 61 ◽  
Author(s):  
Choshun Yoneyama ◽  
Shoufan Cao ◽  
Anna Igual Munoz ◽  
Stefano Mischler
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Layer Structure ◽  
Phosphate Buffer Solution ◽  
Physical Factors ◽  
Low Carbon ◽  
Buffer Solution ◽  
Cocrmo Alloy ◽  
Wear And Friction

Tribocorrosion, as the interaction between mechanical wear and electrochemical corrosion, has been found to be the main problem causing the failure and limiting the lifetime of metal-on-metal artificial hip joints. Better understanding of the tribocorrosion mechanisms of CoCrMo alloys is needed in order to reduce the degradation of this alloy, especially in the presence of proteins as one of the organic components present in synovial fluid. In this study, tribocorrosion tests of a low carbon CoCrMo alloy in phosphate buffer solution (PBS) with and without bovine serum albumin (BSA) in two different concentrations at different applied potentials (passive and cathodic) were carried out. The results show that the effect of proteins on wear and friction was concentration and potential dependent. In the cathodic domain (absence of very thin passive film), wear was very low in all solutions and the friction was significantly reduced by the addition of BSA to PBS even at low BSA concentrations. However, in the passive domain, the friction and wear were found not to be affected when the BSA concentration was 0.5 g/L, while they were reduced when increasing the BSA concentration to 36 g/L. The tribocorrosion results were rationalized through an existing tribocorrosion model and the effect of BSA on wear and friction was explained by the consideration of physical factors such as changes in viscosity and double layer structure, because in the present results no tribofilm formation was observed.

scholarly journals Synthesis of a 5-Carboxy Indole-Based Spiropyran Fluorophore: Thermal, Electrochemical, Photophysical and Bovine Serum Albumin Interaction Investigations

Chemosensors ◽  
2020 ◽  
Vol 8 (2) ◽  
pp. 31
Author(s):  
Rodrigo da Costa Duarte ◽  
Fabiano da Silveira Santos ◽  
Bruno Bercini de Araújo ◽  
Rodrigo Cercena ◽  
Daniela Brondani ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Theoretical Calculations ◽  
Energy Levels ◽  
Phosphate Buffer Solution ◽  
Ultraviolet Region ◽  
Buffer Solution ◽  
Excellent Thermal Stability ◽  
Suppression Mechanism

In this study, we synthesized a spiropyran containing an electron-withdrawing carboxyl group in good yield by condensation of an aromatic aldehyde with enamine indole. The spiropyran absorbed at the ultraviolet region with a maximum at approximately 300 nm, demonstrating slight solvatochromism (~3 nm). A fluorescent emission around 360 nm was observed with a higher solvatochromic effect (~12 nm), indicating higher electronic delocalization in the excited state. The photoreversibility of the open and closed forms of spiropyran excited at 300 nm and 365 nm was not observed, indicating that the absence of the nitro group plays a fundamental role in this equilibrium. Theoretical calculations were also applied for better understanding the photophysics of these compounds. Electrochemical characterization revealed the values of the HOMO and LUMO energy levels at −1.89 eV (electron affinity) and −5.61 eV (ionization potential), respectively. Thermogravimetric analysis showed excellent thermal stability of the spiropyran, with 5% weight loss at approximately 250 °C. Finally, the photophysical features were used to explore the interaction of spiropyran with bovine serum albumin in a phosphate buffer solution, where a significant suppression mechanism was observed.

Effects of Cereal Prolamin Peptides on Differentiated CaCo-2 Cells

1996 ◽  
Vol 24 (4) ◽  
pp. 547-552
Author(s):  
Claudio Giovannini ◽  
Roberto Luchetti ◽  
Elena Mancini ◽  
Massimo de Vincenzi
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Cell Viability ◽  
Mtt Assay ◽  
Bovine Serum ◽  
Cytotoxic Effect ◽  
Cell Damage ◽  
Inhibitory Effect ◽  
Culture Cell ◽  
Glycoprotein Synthesis

The effects of peptic-tiyptic (PT) digests of prolamins derived from several cereals on differentiated CaCo-2 cells were studied on the nineteenth day of culture. Cell viability was determined by using the MTT assay and the colony-forming ability method. The metabolic consequences of peptide exposure were evaluated by measuring RNA, protein and glycoprotein synthesis. While PT digests from bovine serum albumin and durum wheat did not exert any effects, those derived from bread wheat, barley, rye and oats caused a dramatic inhibitory effect on metabolic synthesis and, when measured by using the colony-forming technique, a decrease in cell viability. The MTT assay did not indicate any changes in cell viability. These observations support the hypothesis that, although prolamin-derived peptides from these cereals do not exert an immediate cytotoxic effect, they are responsible for cell damage by impairment of metabolic processes.

scholarly journals Formation of Tribofilm in the Friction of Fluorinated Diamond-Like Carbon (FDLC) Film against Ti6Al4V in Bovine Serum Albumin (BSA) Solution

Coatings ◽  
2020 ◽  
Vol 10 (9) ◽  
pp. 903
Author(s):  
Tengfei Zhang ◽  
Zhaoying Xu ◽  
Yongyao Su ◽  
Jinbiao Wang ◽  
Lu Li ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Phosphate Buffer Solution ◽  
Diamond Like Carbon ◽  
Buffer Solution ◽  
Dlc Film ◽  
System A ◽  
Counterpart Material ◽  
Ball On Disc

A route to reducing the wear of the metal counterpart in the friction of meatal against diamond-like carbon (DLC) is to form a lubricating tribofilm on the metal counterface. However, in liquid lubricating conditions, the formation of tribofilm can be influenced by both the lubricating medium and the counterpart material. Here we report the effect of lubricating biomolecule and doping fluorine element on the formation of tribofilm in fluorinated DLC (FDLC)-Ti6Al4V friction system. A group of ball-on-disc frictional experiments with different sliding speeds and normal loads were performed in phosphate buffer solution (PBS) and bovine serum albumin (BSA) solution. The results showed the formation of tribofilm was inhibited by the absorption of biomolecules on the frictional surface, thus improving the friction coefficient and wear of Ti6Al4V counterpart. Doping fluorine into DLC film also can restrain the formation of tribofilm on Ti6Al4V counterface. As a result, tribofilm is difficult to form when Ti6Al4V counterface slides against FDLC in BSA solution. Fluorinated DLC film should be considered carefully for the anti-wear use in body fluid containing biomolecules because it might cause severe wear of the counterpart material.

scholarly journals Evidence for the involvement of the Ss protein of the mouse in the hemolytic complement system.

1975 ◽  
Vol 141 (5) ◽  
pp. 1216-1220 ◽  
Author(s):  
T H Hansen ◽  
H S Shin ◽  
D C Shreffler
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Complement System ◽  
Bovine Serum ◽  
Specific Antigen ◽  
Mouse Serum ◽  
Antigen Antibody

A significant within-strain correlation has been demonstrated between the levels of Ss and hemolytic complement (C) activity in two Ss-high strains. Mouse serum specifically depleted of Ss by absorption with F(ab')2 fragments of anti-Ss had negligible C activity. In control experiments, Ss-specific antigen-antibody complexes formed with F(ab')2 fragments did not fix rabbit C, and bovine serum albumin-specific antigen-antibody complexes formed with F(ab')2 fragments did not fix mouse C. Therefore the removal of C activity by anti-Ss [F(ab')2] was apparently not due to C fixation. These results suggest that the Ss protein is a necessary component of the C system.

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.

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.

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