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Antimicrobial Peptide Dendrimer Chimera
Author(s) -
Siriwardena Thissa N.,
Lüscher Alexandre,
Köhler Thilo,
van Delden Christian,
Javor Sacha,
Reymond JeanLouis
Publication year - 2019
Publication title -
helvetica chimica acta
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.74
H-Index - 82
eISSN - 1522-2675
pISSN - 0018-019X
DOI - 10.1002/hlca.201900034
Subject(s) - acinetobacter baumannii , chemistry , chimera (genetics) , antimicrobial , klebsiella pneumoniae , pseudomonas aeruginosa , peptide , bacteria , microbiology and biotechnology , dendrimer , antimicrobial peptides , staphylococcus aureus , escherichia coli , biochemistry , biology , gene , genetics , organic chemistry
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.