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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