Human thrombin allows for the in vitro quantitative determination of human TM concentrations in serum, plasma and other biological fluids.Thrombin is an enzyme resulting from activation of prothrombin, which catalyzes the conversion of fibrinogen to fibrin. It is also a potent stimulus to the aggregation of platelets.
People have developed an aptamer-based microarray for human thrombin detection exploiting two non-overlapping DNA thrombin aptamers recognizing different exosites of the target protein. The 15-mer aptamer binds the fibrinogen-binding site, whereas the 29-mer aptamer binds the heparin binding domain. Extensive analysis on the complex formation between human thrombin and modified aptamers was performed by Electrophoresis Mobility Shift Assay, in order to verify in solution whether the chemical modifications introduced would affect aptamers/protein recognition. The validated system was then applied to the aptamer microarray, using the solid phase system devised by the solution studies. Finally, the best procedure for Sandwich Aptamer Microarray and the specificity of the sandwich formation for the developed aptasensor for human thrombin were optimized.
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