Ruth, Deborah M., McMahon, Gillian and Ó Fágáin, Ciarán (2006) Peptide synthesis by recombinant Fasciola hepatica cathepsin L1. Biochimie, 88 (1). pp. 117-120. ISSN 0300-9084
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.
Metadata
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 Institutes 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 19 Jul 2018 14:40 |
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