INVESTIGATION OF THE EFFECTS OF SURFACE-IMMOBILIZED APTAMER END GROUPS ON APTAMER-PROTEIN INTERACTIONS BY MASS SPECTROMETRY

摘要

In the case of thiol modified thrombin aptamers, highly abundant signals of specific thrombin fragments were observed in the masss pectra especially for 6 thymine base units containing aptamer when compared with the other shaving 3 and 12 adenin base units. For thiol modified thrombin aptamers, It was observed that the most efficient thrombin adsorption can be obtained in the case of 3 adenine base unit containing one in comparison with 6 and 12 adenin base containing aptamers. The highest capacity of thrombin adsorption with speccific affinity could be obtained by 6 thymine and 12 adenine base units containing amine modified aptamers from 5' ends.