Research paper

Chemical synthesis of a pore-forming antimicrobial protein, caenopore-5, by using native chemical ligation at a Glu-Cys site

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Title
Chemical synthesis of a pore-forming antimicrobial protein, caenopore-5, by using native chemical ligation at a Glu-Cys site
Content partner
The University of Auckland Library
Collection
ResearchSpace@Auckland
Description

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 ...

Format
Research paper
Research format
Journal article
Date created
2015-01-19
Creator
Medini, Karima / Harris, Paul / Hards, K / Dingley, Andrew / Cook, GM / Brimble, Margaret
URL
http://hdl.handle.net/2292/27380
Related subjects
Cell Membrane / Animals / Caenorhabditis elegans / Caenorhabditis elegans Proteins / Recombinant Proteins / Anti-Infective Agents / Circular Dichroism / Magnetic Resonance Spectroscopy / Amino Acid Sequence / Protein Structure, Secondary / Protein Folding / Permeability / Molecular Sequence Data / Chemistry Techniques, Synthetic / Solid-Phase Synthesis Techniques

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