Molecular recognition of enzymatic active sites is the basis for amultitude of therapeutic interactions. It has been shown that theseinteractions can be strengthened by tethering a molecule with affinity for aneighboring region, to the primary inhibitor. Garnering from this, we havedeveloped nucleic acid chimeras consisting of the inhibiting small moleculesand functional oligonucleotide sequences. Initially, we have studied the efficiencyof this system with the serine protease, trypsin. Association of the chimerawith trypsin has been characterized by fluorescence polarization. Further, weinvestigate whether nucleic acids can be a mechanism for the encouragement ofinhibitor selectivity.

Modulating protein recognition with nucleic acid inputs

239th National Meeting (2010)

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