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© K. Melican.
Human microvessel (red) colonized by N. meningitidis (green).
Publication : Journal of medicinal chemistry

Proteolytically stable foldamer mimics of host-defense peptides with protective activities in a murine model of bacterial infection

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Journal of medicinal chemistry - 16 Aug 2016

Teyssières E, Corre JP, Antunes S, Rougeot C, Dugave C, Jouvion G, Claudon P, Mikaty G, Douat C, Goossens PL, Guichard G

Link to Pubmed [PMID] – 27529632

J. Med. Chem. 2016 Aug;

The synthesis of bio-inspired unnatural backbones leading to foldamers can provide effective peptide mimics with improved properties in a physiological environment. This approach has been applied to the design of structural mimics of membrane active antimicrobial peptides (AMPs) for which activities in vitro have been reported. Yet activities and pharmacokinetic properties in vivo in animal models have remained largely unexplored. Here, we report helical oligourea AMP mimics that are active in vitro against bacterial forms of B. anthracis encountered in vivo, as well as in vivo in inhalational and cutaneous mouse models of B. anthracis infection. The pharmacokinetic profile and the tissue distribution were investigated by beta-radio imager whole-body mapping in mice. Low excretion and recovery of the native oligourea in the kidney following intravenous injection is consistent with high stability in vivo. Overall these results provide useful information that support future biomedical development of urea-based foldamer peptide mimics.

http://www.ncbi.nlm.nih.gov/pubmed/27529632