Non-Carbohydrate Glycomimetics as Inhibitors of the Bacterial Lectin Leca

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1st EuroCarb Young Researcher (ECYR) Workshop

CarboMet Workshop

Mini symposium: Glycobiology at the LUMC and beyond

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Non-Carbohydrate Glycomimetics as Inhibitors of the Bacterial Lectin Leca

Eike Siebs 1,2,3 , Elena Shanina 4,5 , Sakonwan Kuhaudomlarp 6 , Ines Joachim 1,2,3 , Jérémie Topin 6 , Aline Thomas 6 , Christoph Rademacher 4,5 , Anne Imberty 6 , Alexander Titz 1,2,3

1 Chemical Biology of Carbohydrates (CBCH), Helmholtz-Institute for Pharmaceutical Research Saarland (HIPS), Saarbrücken, Germany, 2 Department of Pharmacy, Saarland University, Saarbrücken, Germany, 3 Deutsches Zentrum für Infektionsforschung (DZIF), Braunschweig, Germany, 4 Structural Glycobiology, Max-Planck-Institute for Colloids and Interfaces, Potsdam, Germany, 5 Free University Berlin, Berlin, Germany, 6 Univ. Grenoble Alpes, CNRS, CERMAV, Grenoble, France

Drug resistance is becoming a rising problem worldwide that led to more than 700 000 deaths last year. The opportunistic ESKAPE pathogen Pseudomonas aeruginosa is considered as particularly critical by the World Health Organization (WHO). Different approaches for treatment are currently being investigated and the inhibition of their adhesins to prevent bacterial biofilm formation is a promising approach to break antimicrobial resistance.[1,2] Biofilms protect the bacteria from external threats such as antibiotics and immune defense and are therefore a target for intervention.[3] P. aeruginosa expresses two lectins, D-galactose binding LecA and L-fucose/ D-mannose binding LecB, which are both virulence factors and responsible for bacterial adhesion and biofilm formation. It was shown that inhibition of these lectins with carbohydrate-derived molecules leads to a reduced biofilm formation. Here, we aimed at the development of non-carbohydrate glycomimetics targeting LecA. To this end, we identified catechols as potential LecA inhibitors, and carefully validated these well-known pan assay interference class of molecules in biophysical assays. Competitive binding was established for a distinct set of catechol containing molecules.

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