Documentation scienceplus.abes.fr version Bêta

À propos de : Human Serum Albumin Adsorption on TiO2 from SingleProtein Solutions and from Plasma        

AttributsValeurs
type
Is Part Of
Subject
Title
  • Human Serum Albumin Adsorption on TiO2 from SingleProtein Solutions and from Plasma
has manifestation of work
related by
Author
Abstract
  • In the present work, the adsorption of human serum albumin (HSA) on commercially pure titanium witha titanium oxide layer formed in a H2O2 solution (TiO2 cp) and on TiO2 sputtered on Si (TiO2 sp) wasanalyzed. Adsorption isotherms, kinetic studies, and work of adhesion determinations were carried out.HSA exchangeability was also evaluated. Surface characterization was performed by atomic force microscopy(AFM), X-ray photoelectron spectroscopy (XPS), and wettability studies. The two TiO2 surfaces have verydistinct roughnesses, the TiO2 sp having a mean Ra value 14 times smaller than the one of TiO2 cp. XPSanalysis revealed consistent peaks representative of TiO2 on sputtered samples as well as on Ti cp substrateafter 48 h of H2O2 immersion. Nitrogen was observed as soon as protein was present, while sulfur, presentin disulfide bonds in HSA, was observed for concentrations of protein higher than 0.30 mg/mL. The workof adhesion was determined from contact angle measurements. As expected from the surface free energyvalues, the work of adhesion of HSA solution is higher for the TiO2 cp substrate, the more hydrophilic one,and lower for the TiO2 sp substrate, the more hydrophobic one. The work of adhesion between plasma andthe substrates assumed even higher values for the TiO2 cp surface, indicating a greater interaction betweenthe surface and the complex protein solutions. Adsorption studies by radiolabeling of albumin (125I−HSA)suggest that rapid HSA adsorption takes place on both surfaces, reaching a maximum value after ∼60min of incubation. For the higher HSA concentrations in solution, a multilayer coverage was observed onboth substrates. After the adsorption step from single HSA solutions, the exchangeability of adsorbed HSAmolecules by HSA in solution was evaluated. The HSA molecules adsorbed on TiO2 sp seem to be moreeasily exchanged by HSA itself than those adsorbed on TiO2 cp after 24 h. In contrast, after 72 h, nearlyall the adsorbed albumin molecules effectively exchange with other albumin molecules.
article type
is part of this journal



Alternative Linked Data Documents: ODE     Content Formats:       RDF       ODATA       Microdata