%0 Journal Article
%A Medini, Karima
%A Harris, Paul W R
%A Hards, Kiel
%A Dingley, Andrew
%A Cook, Gregory M
%A Brimble, Margaret A
%T Chemical synthesis of a pore-forming antimicrobial protein, caenopore-5, by using native chemical ligation at a glu-cys site.
%J ChemBioChem
%V 16
%N 2
%@ 1439-4227
%C Weinheim
%I Wiley-VCH
%M FZJ-2016-01839
%P 328 - 336
%D 2015
%X 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.
%K Anti-Infective Agents (NLM Chemicals)
%K Caenorhabditis elegans Proteins (NLM Chemicals)
%K Recombinant Proteins (NLM Chemicals)
%F PUB:(DE-HGF)16
%9 Journal Article
%$ pmid:25425108
%U <Go to ISI:>//WOS:000347780800019
%R 10.1002/cbic.201402513
%U https://juser.fz-juelich.de/record/283506