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Issue 11, 2013
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Glycopeptide dendrimers as Pseudomonas aeruginosa biofilm inhibitors

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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.

Graphical abstract: Glycopeptide dendrimers as Pseudomonas aeruginosa biofilm inhibitors

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Publication details

The article was received on 10 Dec 2012 and first published on 01 Feb 2013

Article type: Review Article
DOI: 10.1039/C3CS35504G
Chem. Soc. Rev., 2013,42, 4814-4822

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    Glycopeptide dendrimers as Pseudomonas aeruginosa biofilm inhibitors

    J. Reymond, M. Bergmann and T. Darbre, Chem. Soc. Rev., 2013, 42, 4814
    DOI: 10.1039/C3CS35504G

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