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082 _ _ |a 540
100 1 _ |a Medini, Karima
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245 _ _ |a Chemical synthesis of a pore-forming antimicrobial protein, caenopore-5, by using native chemical ligation at a glu-cys site.
260 _ _ |a Weinheim
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520 _ _ |a 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.
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650 _ 7 |a Caenorhabditis elegans Proteins
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650 _ 7 |a Recombinant Proteins
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700 1 _ |a Harris, Paul W R
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700 1 _ |a Hards, Kiel
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700 1 _ |a Dingley, Andrew
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700 1 _ |a Cook, Gregory M
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700 1 _ |a Brimble, Margaret A
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773 _ _ |a 10.1002/cbic.201402513
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