texes bearing aldehyde (7), carboxylic (6-8), sulfhydryl The adsorption of bovine serum albumin (BSA) onto polysty- (9), or amino groups (10) to provide covalent immobilizarene latexes bearing various amounts of sugar moieties has been tion of the proteins have been prepared. However, it was investi
Adsorption of Bovine Serum Albumin onto TiO2Particles
โ Scribed by Carla E. Giacomelli; Marcelo J. Avena; Carlos P. De Pauli
- Publisher
- Elsevier Science
- Year
- 1997
- Tongue
- English
- Weight
- 200 KB
- Volume
- 188
- Category
- Article
- ISSN
- 0021-9797
No coin nor oath required. For personal study only.
โฆ Synopsis
The adsorption of bovine serum albumin (BSA) at the TiO 2it is not the sole criterion. Compatibility also depends largely aqueous NaCl interface was studied as a function of pH and elecon what protein the surface denatures and in what sequence. trolyte concentration using kinetic and steady-state measure-For example, low-temperature isotropic carbon, which is a ments. The electrokinetic properties of BSA-covered TiO 2 particles good blood-compatible material, first adsorbs and denatures and the acid-base character of the protein were monitored by albumin in blood and passivates the substrate, preventing electrophoretic mobilities and acid-base potentiometric titration, the activation of blood coagulation proteins. Since during respectively. Some experiments were also outlined to analyze the implantation, proteins and macromolecules from the body different affinities of BSA monomers, dimers, and polymers for the surface. The adsorption process is fast; less than 10 min is fluids adsorb, and may promote or inhibit hemocompatibilenough to achieve steady-state conditions. All measured isotherms ity, a basic study of protein adsorption onto TiO 2 particles showed high initial slopes even under adverse electrostatic condicould contribute to elucidating the mechanisms involved in tions, resulting in high-affinity isotherms. Adsorption plateau valtitanium biocompatibility. Although titanium implantation ues ( G max ) had a great pH dependence; G max -pH curves reached has been reported in clinical studies lasting up to 25 years, a maximum at around the isoelectric point of BSA and showed a there are in the literature only a few works concerning prodrastic decrease on the acid side. Both structural and electrostatic tein adsorption on TiO 2 surfaces. In fact, most of the protein effects must be invoked to explain the diminution of adsorbed adsorption studies performed on inorganic surfaces involve BSA on either side of the isoelectric point. Structural effects were mainly to silica particles (7,(10)(11)(12)(13)(14)(15)(16)(17)(18), to a lower extent hemarelated to the different conformational states that BSA molecules tite (16, 19-21), and in a few, hydroxyapatite (22,23) or adopt with pH changes, whereas electrostatic effects were analyzed assuming that BSA molecules behave as soft particles. This reason-TiO 2 (2)(3)(4)18).
ing also allows us to explain the independence of the G max -pH A survey of the literature (20,(24)(25)(26) shows that several curves from electrolyte concentration.
๐ SIMILAR VOLUMES
The adsorption of bovine serum albumin (BSA) onto relatively hydrophobic TiO 2 surfaces was studied by ellipsometry as a function of pH and BSA concentration. Titanium oxide layers were electrochemically grown on Ti disc electrodes. When fast attachment of BSA onto TiO 2 takes place, the adsorption
The purpose of the study was to characterize mucosal attachment of a cationized model protein, bovine serum albumin (BSA), onto the various fractions of colonic crypts epithelium in the rat. BSA was labeled with ยฏuorescein isothiocyanate (FITC) and its surface net electric charge was modiยฎed from ne