TY  - JOUR
AU  - Medini, Karima
AU  - Harris, Paul W R
AU  - Hards, Kiel
AU  - Dingley, Andrew
AU  - Cook, Gregory M
AU  - Brimble, Margaret A
TI  - Chemical synthesis of a pore-forming antimicrobial protein, caenopore-5, by using native chemical ligation at a glu-cys site.
JO  - ChemBioChem
VL  - 16
IS  - 2
SN  - 1439-4227
CY  - Weinheim
PB  - Wiley-VCH
M1  - FZJ-2016-01839
SP  - 328 - 336
PY  - 2015
AB  - 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.
KW  - Anti-Infective Agents (NLM Chemicals)
KW  - Caenorhabditis elegans Proteins (NLM Chemicals)
KW  - Recombinant Proteins (NLM Chemicals)
LB  - PUB:(DE-HGF)16
C6  - pmid:25425108
UR  - <Go to ISI:>//WOS:000347780800019
DO  - DOI:10.1002/cbic.201402513
UR  - https://juser.fz-juelich.de/record/283506
ER  -