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Antimicrobial Peptide Dendrimer Chimera

Type of publication Peer-reviewed
Publikationsform Original article (peer-reviewed)
Author Siriwardena Thissa N., Lüscher Alexandre, Köhler Thilo, van Delden Christian, Javor Sacha, Reymond Jean‐Louis,
Project Chemical Space Design of Small Molecules and Peptides
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Original article (peer-reviewed)

Journal Helvetica Chimica Acta
Volume (Issue) 102(4)
Page(s) e1900034 - e1900034
Title of proceedings Helvetica Chimica Acta
DOI 10.1002/hlca.v102.4

Abstract

We recently reported the discovery of antimicrobial peptide dendrimers (AMPDs) acting by a membrane-disruptive mechanism against multidrug resistant pathogenic bacteria. Here, we combined amino acid sequence elements from different AMPDs with different activity profiles to form AMPD chimeras. By joining the outer branches of TNS18, an AMPD active against Pseudomonas aeruginosa, Acinetobacter baumannii and methicillin resistant Staphylococcus aureus, with the core of T7, another AMPD active against P. aeruginosa, A. baumannii and Klebsiella pneumoniae, we obtained AMPD chimera DC5 displaying all previously observed activities while retaining a similar mechanism of action. These experiments show that chimera design represents a useful strategy to improve the properties of AMPDs.
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