Adsorption of plasma proteins to the derivatives of polyetherurethaneurea carrying tertiary amino groups in the side chains.
Polyetherurethaneureas carrying tertiary amino groups in the side chains were synthesized, quaternized, and heparinized. The adsorption of plasma proteins to the polyurethane derivatives was investigated using Fourier-transform infrared, surface fluorescence, ultraviolet, and circular dichroism spectroscopy. Bovine gamma-globulin and bovine plasma fibrinogen were easily adsorbed to hydrophobic polyurethanes and denatured. It was found that the beta structure was generated during the irreversible conformational change of the proteins on adsorption to hydrophobic polyurethane materials. On the other hand, bovine serum albumin was easily adsorbed to hydrophilic quaternized and heparinized polyurethanes without a serious conformational change. The conclusion was drawn that a polymer material that selectively adsorbs bovine serum albumin in a native state could be antithrombogenic.
D000327:Adsorption; D000818:Animals; D001672:Biocompatible Materials / Q000378:metabolism*; D001798:Blood Proteins / Q000378:metabolism*; D002417:Cattle; D005343:Fibrinolytic Agents; D006018:Glycols / Q000378:metabolism; D066298:In Vitro Techniques; D011140:Polyurethanes / Q000378:metabolism*; D011485:Protein Binding; D011487:Protein Conformation; D012710:Serum Albumin, Bovine / Q000378:metabolism; D013053:Spectrophotometry
D001672:Biocompatible Materials; D001798:Blood Proteins; D005343:Fibrinolytic Agents; D006018:Glycols; D011140:Polyurethanes; D012710:Serum Albumin, Bovine; C044690:polyetherurethane urea