BSA Adsorption on Hydroxyapatite after Thermal Treatment

2007 ◽  
Vol 361-363 ◽  
pp. 127-130 ◽  
Author(s):  
Elena Mavropoulos ◽  
Nilce C.C. da Rocha ◽  
Maria Helena M. Rocha-Leão ◽  
Antonella M. Rossi
Keyword(s):  
Thermal Treatment ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Phosphate Buffer ◽  
Bovine Serum ◽  
Active Sites ◽  
Sorption Process ◽  
Buffer Concentration ◽  
Surface Active ◽  
Bsa Adsorption

Adsorption experiments of bovine serum albumin on hydroxyapatite previously annealed at temperatures up to 1100°C was performed at 37°C and phosphate buffer, pH 6.0. Kinetic process was very efficient and irreversible for low phosphate buffer concentration. Thermal treatment contributed to the decrease of bovine serum albumin immobilization indicating that sorption process depended on HA specific surface area and the number of surface active sites. However, it was verified that particle size was also an important parameter for bovine serum albumin immobilization.

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 Electrochemical characterization and determination of carbamazepine as pharmaceutical standard and tablet content on gold electrode

2014 ◽  
Vol 68 (2) ◽  
pp. 207-212 ◽  
Author(s):  
Nemanja Trisovic ◽  
Bojan Bozic ◽  
Slobodan Petrovic ◽  
Svetlana Tadic ◽  
Milka Avramov-Ivic
Keyword(s):  
Cyclic Voltammetry ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Phosphate Buffer ◽  
Bovine Serum ◽  
Gold Electrode ◽  
Anticonvulsant Drug ◽  
Voltammetric Techniques ◽  
Anodic Behaviour

The anodic behaviour of carbamazepine (CBZ), an anticonvulsant drug, has been studied on gold electrode in 0.1 mol dm-3 phosphate buffer of pH 7.0 by using cyclic voltammetry. It has been found that the value of the oxidative current of pure CBZ at +0.90 V is a linear function of the concentration in a range from 1.0?10-7 to 1.0?10?4 mol dm?3. The detection of CBZ in the concentration of 1.0?10-8 mol dm-3 is among the lowest that have been reported for this drug using voltammetric techniques. CBZ as a content of tablet Galepsine? has been quantitatively determined. It has also been demonstrated that the modification of gold electrode with bovine serum albumin (BSA) results in a decrease of the oxidative peak current due to the binding of the drug to BSA.

Influence of Blocking Agents on Non-Specific Background of Polystyrene Microbeads in Serum Immunoassay

2013 ◽  
Vol 641-642 ◽  
pp. 858-861 ◽  
Author(s):  
Zhi Min Ren ◽  
Xi Nie ◽  
Sheng Shu Ai
Keyword(s):  
Bovine Serum Albumin ◽  
Polyvinyl Alcohol ◽  
Serum Albumin ◽  
Human Serum ◽  
Phosphate Buffer ◽  
Bovine Serum ◽  
Room Temperature ◽  
Tween 20 ◽  
Blocking Agents

In this paper, we used bovine serum albumin and polymer as the blocking agents and investigated the effect of blocking agents on non-specific background of polystyrene microbead that used the human serum immunoassay.The results showed that the nonspecific background is lower by using polymer blocking agents. The best blocking condition was that microbeads were blocked by PVXT (0.5% polyvinyl alcohol PVA, 0.8% polyvinylpyrrolidone, 0.05% Tween-20, PBS phosphate buffer, pH7.0) for two hours at room temperature.

Insights into the interaction of Bovine Serum Albumin with Surface-Active Ionic Liquids in aqueous solution

2020 ◽  
pp. 114537
Author(s):  
Márcia M.S. Alves ◽  
João M.M. Araújo ◽  
Ivo C. Martins ◽  
Ana B. Pereiro ◽  
Margarida Archer
Keyword(s):  
Aqueous Solution ◽  
Ionic Liquids ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Surface Active

Surface chemistry of bovine serum albumin with hematite nanoparticles and its effect on arsenate adsorption

2021 ◽  
Vol 18 (4) ◽  
pp. 177
Author(s):  
A. M. Eid ◽  
Shea Kraemer ◽  
Hind A. Al-Abadleh
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Surface Chemistry ◽  
Adsorption Kinetics ◽  
Bovine Serum ◽  
Active Sites ◽  
Binding Free Energy ◽  
Biological Systems ◽  
Hematite Nanoparticles ◽  
Arsenate Adsorption

Environmental contextHematite nanoparticles are efficient adsorbents for proteins and pollutants in environmental and biological systems. Hematite and the protein bovine serum albumin (BSA) were used as models to investigate the surface chemistry and competitive role of BSA in arsenate adsorption. Results show that surface BSA inhibits arsenate adsorption, potentially altering its mobility and bioavailability. AbstractThe surface chemistry of metal oxide nanomaterials controls their health impacts and fate in environmental and biological systems. These systems contain proteins capable of binding to nanoparticles, which forms a protein corona that modifies the surface properties of the nanoparticles and reactivity towards pollutants. Using attenuated total reflectance-Fourier transform infrared (ATR-FTIR) spectroscopy, we investigate the adsorption of bovine serum albumin (BSA) and quantify the competitive effect of BSA on the adsorption kinetics of arsenate, AsV, to hematite nanoparticles. Experiments were conducted in the flow mode at pH 7. BSA was first adsorbed on hematite, then AsV was allowed to flow over the BSA/hematite thin film. Adsorption kinetic and thermodynamic parameters were calculated using a modified Langmuir adsorption model for both BSA and AsV. The adsorption thermodynamic model showed that BSA binds through two active sites with a binding energy of –41 kJ mol−1, which corresponds to the spontaneous formation of chemisorbed and physisorbed species. When AsV flowed over the BSA/hematite film, only 11 % of surface BSA was desorbed by AsV. This result highlights the inhibitory effect of BSA for AsV adsorption. Structural analysis of BSA revealed changes to the local conformational geometry upon adsorption to and desorption from hematite nanoparticles. Molecular docking simulations showed that the binding free energy of a modelled hematite nanoparticle towards the BSA surface is –6.8 kcal mol−1 (−28.5 kJ mol−1) owing to the formation of various bonds, which agrees with the adsorption kinetics modelling. Overall, surface BSA inhibits arsenate adsorption and therefore increases its mobility and bioavailability.

Bovine serum albumin adsorption on passivated porous silicon layers

2004 ◽  
Vol 82 (10) ◽  
pp. 1545-1553 ◽  
Author(s):  
L Tay ◽  
N L Rowell ◽  
D Poitras ◽  
J W Fraser ◽  
D J Lockwood ◽  
...  
Keyword(s):  
Porous Silicon ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Crystalline Silicon ◽  
Electrochemical Anodization ◽  
Undecylenic Acid ◽  
Ft Ir ◽  
Lift Off ◽  
Bsa Adsorption

Hydrogen-terminated porous silicon (pSi-H) films were fabricated through electrochemical anodization of crystalline silicon in hydrofluoric-acid-based solutions. The pSi-H surface was chemically functionalized by thermal reaction with undecylenic acid to produce an organic monolayer covalently attached to the silicon surface through Si—C bonds and bearing an acid terminal group. Bovine serum albumin (BSA) was adsorbed onto such surface-modified pSi structures. The resulting surfaces were characterized using scanning electron microscopy (SEM), reflection FT-IR spectroscopy, and ellipsometry. SEM showed that the porous films were damaged and partially lifted off the silicon substrate after a prolonged BSA adsorption. Ellipsometry analysis revealed that the BSA penetrated ∼1.3 µm into the porous structure. The film damage is likely a result of BSA anchoring itself tightly through strong electrostatic interaction with the acid-covered Si sidewalls. A change in surface tension during BSA film formation then causes the pSi layer to buckle and lift off the underlying Si substrate. FT-IR results from the undecylenic-acid-modified pSi surfaces before and after BSA adsorption showed the presence of strong characteristic amide I, II, and III vibrational bands after BSA adsorption. The surface properties of the pSi matrix and its interactions with BSA are examined in this study.Key words: ellipsometry, porous silicon, protein adsorption, surface passivation.

Sign in / Sign up

Export Citation Format

Share Document