Dynamic Aspects of Protein Adsorption onto Titanium Surfaces:  Mechanism of Desorption into Buffer and Release in the Presence of Proteins in the Bulk

Abstract

The release process for adsorbed IgG molecules on titanium particle surfaces in the presence of pure buffer or IgG molecules in solution was investigated by means of radiolabeling techniques. This study is part of a general investigation of the basic mechanisms underlying exchange processes of adsorbed proteins by macromolecules in the bulk and in particular of the kinetic laws describing such processes. This study shows the existence, in the investigated time scale (from 1 to 43 h), of two different populations of adsorbed IgG molecules: a population called type I which is releasable from the surface and a type II population which is irreversibly adsorbed on the surface. As in previous studies, we confirm that for the population of type I, the kinetics of the release mechanism is enhanced by the presence of IgG molecules in solution. This is a strong indication that it constitutes an exchange process. Moreover, we show that this release process is of order 1 with respect to both adsorbed and bulk molecules. Finally, we show that the percentage of molecules of type I (reversibly adsorbed on the surface at the adsorption time scale investigated) seems to increase linearly with the bulk concentration of proteins during the release experiments, in the investigated bulk concentration range. This unexpected result constitutes a new observation and we do not posses a satisfactory explanation for it. A similar increase was also reported for exchange experiments performed with polyacrylamide onto aluminosilicated glass beads by Pefferkorn et al. (Pefferkorn, E.; Carroy, A.; Varoqui, R. J. Polym. Sci., Polym. Phys. Ed. 1985, 23, 1997).

Electrospray–differential mobility analysis of bionanoparticles

“…On the other hand for IgM desorption from bare silica is 0.004 ± 0.0025 min -1 and 0.00035 ± 0.00007 min -1 for monomers and dimers respectively. These values are well within the wide range of desorption rate constants (≈10 -4 min -1 to ≈1 min -1 ) found in the literature [120,[144][145][146]. Clearly, there are two important inferences: the monomer desorbs faster than the dimer for both surfaces, and the propensity for both the monomers and dimers of IgM to stay adsorbed on the gelatin-passivated surface is lower.…”

“…The desorption rate constants are listed in Table 4.1. Using X-ray photoelectron spectroscopy, Ball et al [120] found desorption rate constant for IgG to be ≈ 10 -5 sec -1 , consistent with above results.…”

Optical Detection of Protein Adsorption on Doped Titanium Surface

“…(Ball et al, 1996;Höök et al, 2002a;Huang et al, 2003;Imamura et al, 2008;Jones et al, 2000;Walivaara et al, 1994;Yang et al, 2003) These kind of biomaterial applications made of titanium are satisfactory products, because of their ability to adsorb certain proteins. After implantation, within a few seconds, the biomaterial surface becomes coated with a film of adsorbed proteins mediating the interaction between the implant and the body environment.…”

Fibrinogen and cellular adherability on differently treated titanium as implants

“…Titanium and its alloys are widely used as implants. Titanium belongs to a specific group of materials, which are very stable and have high corrosion resistance and tissue tolerance [1][2][3][4]. This fact is mainly due to the creation of a protective layer formed on air and liquids on surfaces of titanium.…”