Protein Adsorption Properties of Hydrothermally Prepared Hydroxyapatite

2007 ◽  
Vol 361-363 ◽  
pp. 71-74 ◽  
Author(s):  
Giichiro Kawachi ◽  
T. Watanabe ◽  
K. Kikukta ◽  
Chikara Ohtsuki
Keyword(s):  
Bovine Serum Albumin ◽  
Protein Adsorption ◽  
Bovine Serum ◽  
Phosphate Buffer Solution ◽  
Egg White ◽  
Adsorption Properties ◽  
Phosphate Concentration ◽  
Hydrothermal Processing ◽  
Crystal Face ◽  
Buffer Solution

Micrometer-sized hydroxyapatite (HA) with rod-shape was prepared to investigate protein adsorption onto its crystal face, through hydrothermal processing. Adsorption of Bovine serum albumin (BSA) and Lysozyme from chicken egg white (LSZ) on rod-shaped HA crystals with approximately 50 μm in length and 1 μm thickness was examined in phosphate buffer solution. The amount of adsorbed BSA was decreased with increasing phosphate concentration in the examined solution. Adsorption of LSZ was increased with increasing phosphate concentration in the buffer solution up to 50 mmol/L (mM), while it was remarkably decreased when the phosphate concentration reached approximately 100 mM. These phenomena lead to understanding of chromatographic characters of HA for separation of acidic and basic proteins.

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 The Formation of Polycomplexes of Poly(Methyl Vinyl Ether-Co-Maleic Anhydride) and Bovine Serum Albumin in the Presence of Copper Ions

2014 ◽  
Vol 16 (3) ◽  
pp. 97-105 ◽  
Author(s):  
Mesut Karahan ◽  
Zeynep Mustafaeva ◽  
Cemal Özeroğlu
Keyword(s):  
Bovine Serum Albumin ◽  
Maleic Anhydride ◽  
Phosphate Buffer ◽  
Bovine Serum ◽  
Copper Ions ◽  
Phosphate Buffer Solution ◽  
Buffer Solution ◽  
Methyl Vinyl ◽  
Polymer Metal ◽  
Methyl Vinyl Ether

Abstract The binary and ternary complex formations of poly(methyl vinyl ether-co-maleic anhydride) (PMVEMA) with copper ions and with bovine serum albumin (BSA) in the presence of copper ions in phosphate buffer solution at pH = 7 were examined by the techniques of UV-visible, fluorescence, dynamic light scattering, atomic force microscopy measurements. In the formation of binary complexes of PMVEMA-Cu(II), the addition of copper ions to the solution of PMVEMA in phosphate buffer solution at pH = 7 forms homogeneous solutions when the molar ratio of Cu(II)/MVEMA is 0.5. Then the formations of ternary complexes of PMVEMA-Cu(II)-BSA were examined. Study analysis revealed that the toxicities of polymer-metal and polymer-metal-protein mixture solutions depend on the nature and ratio of components in mixtures.

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.

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.

Use of Magnetic Fe3O4 Nanoparticles Coated with Bovine Serum Albumin for the Separation OF Lysozyme from Chicken Egg white

2021 ◽  
pp. 129442
Author(s):  
Mariane Gonçalves Santos ◽  
Diailison Teixeira de Carvalho ◽  
Lucas Belga Caminitti ◽  
Bruna Bueno Alves de Lima ◽  
Marcello Henrique da Silva Cavalcanti ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Fe3o4 Nanoparticles ◽  
Bovine Serum ◽  
Egg White ◽  
Chicken Egg ◽  
Magnetic Fe3o4 Nanoparticles ◽  
Magnetic Fe3o4

Sensing of Protein Adsorption by Composites Consisting of Silver Nanoparticles and Hydroxyapatite

2010 ◽  
Vol 76 ◽  
pp. 90-99
Author(s):  
Chikara Ohtsuki ◽  
Yuji Ichikawa ◽  
Hiroyuki Shibata ◽  
Tsukasa Torimoto ◽  
Ill Yong Kim
Keyword(s):  
Silver Nanoparticles ◽  
Protein Adsorption ◽  
Phosphate Buffer Solution ◽  
Trisodium Citrate ◽  
Localized Surface Plasmon ◽  
Surface Charges ◽  
Buffer Solution ◽  
Promising Candidate ◽  
Hydroxyapatite Powder ◽  
The Matrix

The sensing of protein adsorption by silver nanoparticles/hydroxyapatite composites was investigated using a phosphate buffer solution containing bovine serum albumin (BSA) or lysozyme (LSZ). The adsorption of BSA and LSZ on the composites prepared without using trisodium citrate was similar to plain hydroxyapatite, whereas composites prepared with trisodium citrate showed lower BSA adsorption and higher LSZ adsorption than plain hydroxyapatite powder. Because the ability of the adsorption is mainly governed by surface charges of the powders, the usage of trisodium citrate during the preparation is assumed to produce high negative charges on the surface. The protein adsorption resulted in peak shifts in localized surface plasmon resonance (LSPR) spectra. The peak shifts clearly corresponded to the concentration of the surrounding proteins up to the point of saturation of adsorption on the hydroxyapatite. The silver nanoparticles/hydroxyapatite composites are promising candidate materials for detection of protein adsorption by measurement of LSPR peak shifts, that may be attributed to changes in the dielectric properties of the matrix fluid surrounding the silver nanoparticles.

Emerging investigator series: protein adsorption and transformation on catalytic and food-grade TiO2 nanoparticles in the presence of dissolved organic carbon

2019 ◽  
Vol 6 (6) ◽  
pp. 1688-1703 ◽  
Author(s):  
Junyeol Kim ◽  
Kyle Doudrick
Keyword(s):  
Titanium Dioxide ◽  
Bovine Serum Albumin ◽  
Organic Carbon ◽  
Serum Albumin ◽  
Surface Chemistry ◽  
Protein Adsorption ◽  
Bovine Serum ◽  
Titanium Dioxide Nanoparticles ◽  
Food Grade ◽  
Exposure History

The adsorption and unfolding behavior of bovine serum albumin onto catalytic- and food-grade titanium dioxide nanoparticles is dependent on the surface chemistry of the nanoparticles and their environmental exposure history.

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.

Conformational Change of Protein due to Contact with Bioceramic Materials

2005 ◽  
Vol 284-286 ◽  
pp. 517-520 ◽  
Author(s):  
Satoshi Nagai ◽  
Kanji Tsuru ◽  
Satoshi Hayakawa ◽  
Akiyoshi Osaka
Keyword(s):  
Structural Change ◽  
Secondary Structure ◽  
Bovine Serum Albumin ◽  
Protein Adsorption ◽  
Tricalcium Phosphate ◽  
Bovine Serum ◽  
Adsorption Property ◽  
Cd Spectroscopy ◽  
Uv Spectra ◽  
Interaction Forces

The structural change of bovine serum albumin (BSA) was analyzed by means of ultraviolet (UV) and circular dichroism (CD) spectroscopy due to in contact with ceramics powders such as Al2O3, SiO2, TiO2, ZrO2, hydroxyapatite and b-tricalcium phosphate. The absorbance of the UV spectra increased for the BSA solution in contact with TiO2, ZrO2 and Al2O3, that is, the BSA solution clouded. This indicated the aggregation of BSA after contact with those ceramics powders. The CD spectroscopy showed that the ordered secondary structure of BSA was diminished on contact with TiO2 and ZrO2. We discussed the protein adsorption property of ceramics on the basis of the magnitude of the interaction forces between proteins and the bioceramics.

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