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@ARTICLE{Medini:283506,
      author       = {Medini, Karima and Harris, Paul W R and Hards, Kiel and
                      Dingley, Andrew and Cook, Gregory M and Brimble, Margaret A},
      title        = {{C}hemical synthesis of a pore-forming antimicrobial
                      protein, caenopore-5, by using native chemical ligation at a
                      glu-cys site.},
      journal      = {ChemBioChem},
      volume       = {16},
      number       = {2},
      issn         = {1439-4227},
      address      = {Weinheim},
      publisher    = {Wiley-VCH},
      reportid     = {FZJ-2016-01839},
      pages        = {328 - 336},
      year         = {2015},
      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.},
      keywords     = {Anti-Infective Agents (NLM Chemicals) / Caenorhabditis
                      elegans Proteins (NLM Chemicals) / Recombinant Proteins (NLM
                      Chemicals)},
      cin          = {ICS-6},
      ddc          = {540},
      cid          = {I:(DE-Juel1)ICS-6-20110106},
      pnm          = {553 - Physical Basis of Diseases (POF3-553)},
      pid          = {G:(DE-HGF)POF3-553},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:25425108},
      UT           = {WOS:000347780800019},
      doi          = {10.1002/cbic.201402513},
      url          = {https://juser.fz-juelich.de/record/283506},
}