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Glycopeptide dendrimers as Pseudomonas aeruginosa biofilm inhibitors.

Type of publication Peer-reviewed
Publikationsform Review article (peer-reviewed)
Author Reymond Jean-Louis, Bergmann Myriam, Darbre Tamis,
Project Exploring Peptide Topologies in Search for New Drugs
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Review article (peer-reviewed)

Journal Chemical Society reviews
Volume (Issue) 42(11)
Page(s) 4814 - 22
Title of proceedings Chemical Society reviews
DOI 10.1039/c3cs35504g


Synthetic glycopeptide dendrimers composed of a branched oligopeptide tree structure appended with glycosidic groups at its multiple N-termini were investigated for binding to the Pseudomonas aeruginosa lectins LecB and LecA. These lectins are partly responsible for the formation of antibiotic resistant biofilms in the human pathogenic bacterium P. aeruginosa, which causes lethal airway infections in immune-compromised and cystic fibrosis patients. Glycopeptide dendrimers with high affinity to the lectins were identified by screening of combinatorial libraries. Several of these dendrimers, in particular the LecB specific glycopeptide dendrimers FD2 and d-FD2 and the LecA specific glycopeptide dendrimers GalAG2 and GalBG2, also efficiently block P. aeruginosa biofilm formation and induce biofilm dispersal in vitro. Structure-activity relationship and structural studies are reviewed, in particular the observation that multivalency is essential to the anti-biofilm effect in these dendrimers.