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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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Abstract

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.

Item Type:Article (Published)
Refereed:Yes
Uncontrolled Keywords:fasciola hepatica cathepsin L1; recombinant; enzymatic peptide synthesis; cysteine proteinase;
Subjects:Biological Sciences > Biochemistry
DCU Faculties and Centres:DCU Faculties and Schools > Faculty of Science and Health > School of Chemical Sciences
DCU Faculties and Schools > Faculty of Science and Health > School of Biotechnology
Research Initiatives and Centres > National Centre for Sensor Research (NCSR)
Publisher:Elsevier
Official URL:http://dx.doi.org/10.1016/j.biochi.2005.06.004
Use License:This item is licensed under a Creative Commons Attribution-NonCommercial-Share Alike 3.0 License. View License
ID Code:78
Deposited On:26 Jun 2007 by DORAS Administrator. Last Modified 13 Feb 2017 11:49

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