Chemical synthesis of a pore-forming antimicrobial protein, caenopore-5, by using native chemical ligation at a Glu-Cys site

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dc.contributor.author Medini, Karima en
dc.contributor.author Harris, Paul en
dc.contributor.author Hards, K en
dc.contributor.author Dingley, Andrew en
dc.contributor.author Cook, GM en
dc.contributor.author Brimble, Margaret en
dc.date.accessioned 2015-11-04T01:12:13Z en
dc.date.issued 2015-01-19 en
dc.identifier.citation ChemBioChem: a European journal of chemical biology, 2015, 16 (2), pp. 328 - 336 en
dc.identifier.issn 1439-4227 en
dc.identifier.uri http://hdl.handle.net/2292/27380 en
dc.description.abstract The 2014 report from the World Health Organization (WHO) on antimicrobial resistance revealed an alarming rise in antibiotic resistance all around the world. Unlike classical antibiotics, with the exception of a few species, no acquired resistance towards antimicrobial peptides (AMPs) has been reported. Therefore, AMPs represent leads for the development of novel antibiotics. Caenopore-5 is constitutively expressed in the intestine of the nematode Caenorhabditis elegans and is a pore-forming AMP. The protein (82 amino acids) was successfully synthesised by using Boc solid-phase peptide synthesis and native chemical ligation. No γ-linked by-product was observed despite the use of a C-terminal Glu-thioester. The folding of the synthetic protein was confirmed by (1) H NMR spectroscopy and circular dichroism and compared with data recorded for recombinant caenopore-5. The permeabilisation activities of the protein and of shortened analogues were evaluated. en
dc.description.uri http://www.ncbi.nlm.nih.gov/pubmed/25425108 en
dc.format.medium Print-Electronic en
dc.language English en
dc.publisher Wiley-VCH Verlag en
dc.relation.ispartofseries ChemBioChem: a European journal of chemical biology en
dc.rights Items in ResearchSpace are protected by copyright, with all rights reserved, unless otherwise indicated. Previously published items are made available in accordance with the copyright policy of the publisher. Details obtained from http://www.sherpa.ac.uk/romeo/issn/1439-4227/ http://onlinelibrary.wiley.com/journal/10.1002/(ISSN)1439-7633/homepage/2268_guidel.html en
dc.rights.uri https://researchspace.auckland.ac.nz/docs/uoa-docs/rights.htm en
dc.subject Cell Membrane en
dc.subject Animals en
dc.subject Caenorhabditis elegans en
dc.subject Caenorhabditis elegans Proteins en
dc.subject Recombinant Proteins en
dc.subject Anti-Infective Agents en
dc.subject Circular Dichroism en
dc.subject Magnetic Resonance Spectroscopy en
dc.subject Amino Acid Sequence en
dc.subject Protein Structure, Secondary en
dc.subject Protein Folding en
dc.subject Permeability en
dc.subject Molecular Sequence Data en
dc.subject Chemistry Techniques, Synthetic en
dc.subject Solid-Phase Synthesis Techniques en
dc.title Chemical synthesis of a pore-forming antimicrobial protein, caenopore-5, by using native chemical ligation at a Glu-Cys site en
dc.type Journal Article en
dc.identifier.doi 10.1002/cbic.201402513 en
pubs.issue 2 en
pubs.begin-page 328 en
pubs.volume 16 en
dc.rights.holder Copyright: Wiley-VCH Verlag en
dc.identifier.pmid 25425108 en
pubs.author-url http://onlinelibrary.wiley.com/doi/10.1002/cbic.201402513/full en
pubs.end-page 336 en
pubs.publication-status Published en
dc.rights.accessrights http://purl.org/eprint/accessRights/RestrictedAccess en
pubs.subtype Article en
pubs.elements-id 467907 en
pubs.org-id Science en
pubs.org-id Biological Sciences en
pubs.org-id Chemistry en
pubs.org-id Science Research en
pubs.org-id Maurice Wilkins Centre (2010-2014) en
dc.identifier.eissn 1439-7633 en
pubs.record-created-at-source-date 2015-11-04 en
pubs.dimensions-id 25425108 en


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