Peptide synthesis by recombinant Fasciola hepatica cathepsin L1.
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 degrees 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.
Ruth
Deborah M
DM
School of Biotechnology, National Center for Sensors Research, Dublin City University, Dublin 9, Ireland.
McMahon
Gillian
G
O'Fágáin
Ciarán
C
D000818:Animals; D002403:Cathepsins / Q000378:metabolism*; D002853:Chromatography, Liquid; D005210:Fasciola hepatica / Q000201:enzymology*; D013058:Mass Spectrometry; D009842:Oligopeptides / Q000096:biosynthesis*; D010452:Peptide Biosynthesis; D011994:Recombinant Proteins / Q000378:metabolism
D009842:Oligopeptides; D011994:Recombinant Proteins; C508046:benzyloxycarbonyl-phenylalanyl-arginyl-serinamide; D002403:Cathepsins