Peptide synthesis by recombinant Fasciola hepatica cathepsin L1
Ruth, Deborah M. and McMahon, Gillian and Ó'Fágáin, Ciarán (2006) Peptide synthesis by recombinant Fasciola hepatica cathepsin L1. Biochimie, 88 (1). pp. 117-120. ISSN 0300-9084
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Synthesis of the tripeptide Z-Phe-Arg-SerNH2 has been accomplished by a recombinant cysteine protease, cathepsin L1 from liver fluke (Fasciola hepatica), using Z-Phe-Arg-OMe as acyl acceptor and SerNH2 as nucleophile in 0.1 M ammonium acetate pH 9.0–12.5% v/v acetonitrile at 37 °C. LC–MS detection indicated tripeptide formation after 10 min, continuing up to 5.5 h. The ester Z-Phe-Arg-OMe was detected throughout the experiment but the hydrolysis product Z-Phe-Arg-OH appeared early and in quite large amounts. We believe that this is the first application of a parasite protease in enzymatic peptide synthesis.
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