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000283506 1001_ $$0P:(DE-HGF)0$$aMedini, Karima$$b0
000283506 245__ $$aChemical synthesis of a pore-forming antimicrobial protein, caenopore-5, by using native chemical ligation at a glu-cys site.
000283506 260__ $$aWeinheim$$bWiley-VCH$$c2015
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000283506 520__ $$aThe 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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000283506 650_7 $$2NLM Chemicals$$aAnti-Infective Agents
000283506 650_7 $$2NLM Chemicals$$aCaenorhabditis elegans Proteins
000283506 650_7 $$2NLM Chemicals$$aRecombinant Proteins
000283506 7001_ $$0P:(DE-HGF)0$$aHarris, Paul W R$$b1
000283506 7001_ $$0P:(DE-HGF)0$$aHards, Kiel$$b2
000283506 7001_ $$0P:(DE-Juel1)145681$$aDingley, Andrew$$b3$$ufzj
000283506 7001_ $$0P:(DE-HGF)0$$aCook, Gregory M$$b4
000283506 7001_ $$0P:(DE-HGF)0$$aBrimble, Margaret A$$b5$$eCorresponding author
000283506 773__ $$0PERI:(DE-600)2020469-3$$a10.1002/cbic.201402513$$gVol. 16, no. 2, p. 328 - 336$$n2$$p328 - 336$$tChemBioChem$$v16$$x1439-4227$$y2015
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