The establishment of an aptamer-based biochip for protein detection is described. Using a model system comprising human IgE as the analyte and single-stranded DNA aptamers specific for IgE or anti-IgE antibodies as immobilized ligands on chips, we could demonstrate that aptamers were equivalent or superior to antibodies in terms of specificity and sensitivity, respectively. Aptamer-based analyte detection on glass slides could clearly be demonstrated at minimum concentrations of 10 ng/mL IgE. In addition, we successfully showed specific analyte recognition in complex protein samples by the aptamer-based biochip system. Using DNA aptamers specific for human thrombin as an additional model receptor/ligand system, dual protein detection on a single slide could be proven. In conclusion, we could show the suitability of nucleic acid aptamers as low molecular weight receptors on biochips for sensitive and specific protein detection, representing an innovative tool for future proteomics.
The surface of foils and vascular grafts made from a thermoplastic polycarbonate urethanes (PCU) (Chronoflex AR) were chemically modified using gas plasma treatment, binding of hydrogels—(1) polyethylene glycol bisdiamine and carboxymethyl dextran (PEG-DEX) and (2) polyethyleneimine (PEI)—and immobilization of human antithrombin III (AT). Their biological impact was tested in vitro under static and dynamic conditions. Static test methods showed a significantly reduced adhesion of endothelial cells, platelets, and bacteria, compared to untreated PCU. Modified PCU grafts were circulated in a Chandler-Loop model for 90 min at 37 °C with human blood. Before and after circulation, parameters of the hemostatic system (coagulation, platelets, complement, and leukocyte activation) were analyzed. PEI-AT significantly inhibited the activation of both coagulation and platelets and prevented the activation of leukocytes and complement. In conclusion, both modifications significantly reduce coagulation activation, but only PEI-AT creates anti-bacterial and anti-thrombogenic functionality.
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