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In vitro display technologies are powerful tools for isolating polypeptide binders against various target molecules. The mRNA display approach to in vitro protein selection is based upon the puromycin-mediated formation of a covalent bond between an mRNA and its gene product. In this paper, we use mRNA display to isolate peptides that bind thymidylate synthase (TS) RNA with high affinity from a large peptide library (>1013 different sequences). The selection scheme was constructed, and the experimental conditions, including library synthesis, formation and isolation of RNA-peptide fusions were optimized. mRNA display could play a key role in the discovery of peptides with desired functions.