Aptamers can be selected to be highly specific and to have high affinities for their targets. They are also very stable to heat and long-term storage. The added advantage that aptamers generally change in structure upon binding their specific ligand makes it possible to incorporate them into a variety of analytical devises. The Nilsen-Hamilton lab has collaborated with several groups to select new aptamers, to understand how their structures are influenced by ligand binding, and to develop analytical instruments that use aptamers to detect biological compounds and chemicals.
Aptamer selection is being done in collaboration with the Maury and Przytycka groups. We collaborate with the Lamm group to explore aptamer structure and how it is altered by ligand. These studies have demonstrated that the malachite green aptamer can close down so completely on their ligands that even a hydroxyl cannot gain access to the central carbon malachite green when it is bound by the aptamer. The development of instrumentation that relies on aptamers for detection is being done in collaboration with the Shrotriya and Kraus groups. Our current aptamer targets for detection are Ebola virus proteins.