Molecule of the Month
July 2016
Structural Insight into Glycopeptide Dendrimer Lectin Interactions

We recently discovered peptide dendrimers with strong activity against multidrug-resistant bacteria such as Pseudomonas aeruginosa and their biofilms. In the course of these investigations we obtained the first high resolution X-ray crystal structure of a peptide dendrimer in form of a complex with the virulence factor LecB, a fucose specific lectin [1]. This structure reveals a supramolecular trimeric structure linked via β-sheets.
Our work with antimicrobial peptide dendrimers further extends to applications in the area of burn wound bandage formulations in collaboration with the TransMed B5 Platform Project [2].

This work was carried out in the group of Prof. Jean-Louis Reymond.


  1. G. Michaud, R. Visini, M. Bergmann, G. Salerno, R. Bosco, E. Gillon, B. Richichi, C. Nativi, A. Imberty, A. Stocker, T. Darbre, J.-L. Reymond;
    "Overcoming antibiotic resistance in Pseudomonas aeruginosa biofilms using glycopeptide dendrimers"
    Chem. Sci., 2016, 7(1), 166-182; doi:10.1039/C5SC03635F.
  2. P. Abdel-Sayed, A. Kaeppeli, T. Siriwardena, T. Darbre, K. Perron, P. Jafari, J.-L. Reymond, D. P. Pioletti, L. A. Applegate;
    "Anti-Microbial Dendrimers against Multidrug-Resistant P. aeruginosa Enhance the Angiogenic Effect of Biological Burn-wound Bandages"
    Sci. Rep., 2016, 6, 22020/1-10; doi:10.1038/srep22020.