We describe here a new strategy for isolating target proteins from complex biological samples based on an aptamer-modified self-propelled microtube engine. For this purpose, a thiolated thrombin or a mixed thrombin-ATP aptamer (prehybridized with a thiolated short DNA) was coassembled with mercaptohexanol onto the gold surface of these microtube engines. The rapid movement of the aptamer-modified microtransporter resulted in highly selective and rapid capture of the target thrombin, with an effective discrimination against a large excess of nontarget proteins. Release of the captured thrombin can be triggered by the addition of ATP that can bind and displace the immobilized mixed thrombin-ATP aptamer in 20 min. The rapid loading and unloading abilities demonstrated by these selective microtransporters are illustrated in complex matrixes such as human serum and plasma. The new motion-driven protein isolation platform represents a new approach in bioanalytical chemistry based on active transport of proteins and offers considerable promise for diverse diagnostic applications.
© 2011 American Chemical Society