Research Article abstract


Nature Biotechnology 14, 1116 - 1119 (1996)
doi:10.1038/nbt0996-1116

Mirror-design of L-oligonucleotide ligands binding to L-arginine

Alexis Nolte1, Sven Klus zligmann1, Rolf Bald1, Volker A. Erdmann1 & Jens P. Fürste1, ,*


The high affinity and selectivity of nucleic acid ligands have clearly demonstrated that RNA can be targeted to a variety of molecules. In practice, however, the use of unmodified aptamers is impeded by the low stability of RNA in biological fluids. Here we describe the mirror-design of a stable 38-mer L-oligoribonucleotide ligand that binds to L-arginine. This L-RNA ligand was also able to bind to a short peptide containing the basic region of the human immunodeficiency virus type-1 Tat-protein. The L-RNA ligand displayed the expected stability in human serum. These findings may contribute to the identification of novel diagnostics and pharmaceuticals.

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  1. 1Institut für Biochemie, Freie Universität Berlin, Thielallee 63, D-14195 Berlin, Germany.
  2. *fuerste@chemie.fu-berlin.de