The paper Antimicrobial Peptide Dendrimer Chimera has been accepted by Helvetica Chimica Acta.
We recently reported the discovery of an 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.
Author(s): Thissa Siriwardena, Alexandre Lüscher, Thilo Köhler, Christian van Delden, Sacha Javor, Jean-Louis Reymond