Adsorption of albumin and IgG to porous and smooth titanium.
The possibility to load submicrometer porous titanium surfaces with relatively small proteins, albumin and immunoglobulin G (IgG) was investigated. The loading ability is of interest due to the possibility of slow release of molecules from biomaterial surfaces, and may be important for the manipulation of wound healing around prostheses. Iodine-125 (125I) labeled albumin and IgG were adsorbed onto smooth and to porous titanium with a pore diameter of 200-300 nm. The smooth and porous surfaces were divided into three groups: hydrophilic, hydrophobic, or to amine-terminated silane (3-aminopropyltriethoxysilane) that bound proteins via glutaraldehyde. The protein solution pH and protein concentrations were varied, and the adsorption experiments made without or in the presence of calcium and magnesium ions. The adsorbed amounts were quantified with a gamma counter. Two to eleven times more proteins adsorbed onto porous than smooth surfaces and the adsorbed amounts increased with increasing protein concentration (0.1-10 mg/ml) during a constant incubation time. The elutability by sodium dodecyl sulphate (SDS) was incomplete on porous surfaces.
Jansson
Eva
E
Laboratory of Applied Physics, Department of Physics and Measurement Technology, Linköping University, SE-581 83 Linköping, Sweden.
Tengvall
Pentti
P
D000327:Adsorption; D000418:Albumins / Q000737:chemistry*; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007074:Immunoglobulin G / Q000737:chemistry*; D007457:Iodine Radioisotopes; D016062:Porosity; D013499:Surface Properties; D014025:Titanium / Q000737:chemistry*
D000418:Albumins; D007074:Immunoglobulin G; D007457:Iodine Radioisotopes; D014025:Titanium