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Issue 11, 2013

Glycopeptide dendrimers as Pseudomonas aeruginosa biofilm inhibitors

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Abstract

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

Article information


Submitted
10 Dec 2012
First published
01 Feb 2013

Chem. Soc. Rev., 2013,42, 4814-4822
Article type
Review Article

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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