Antiadhesive glycoconjugate metal complexes targeting pathogens <i>Pseudomonas aeruginosa</i> and <i>Candida albicans</i>

Glycoconjugates are known to interact with carbohydrate-binding proteins involved in adhesion by pathogens, and offer opportunities to design antimicrobial agents. Metal complexes with Eu(III), Ni(II) and Zn(II) were prepared from glycoconjugate ligand 1Gal, which binds to <i>P. aeruginosa</i>'s lectin LecA (<i>K</i><sub>d</sub> 9.6 ± 0.7 μM). <i>In vitro</i> anti-adhesive activity of these compounds was evaluated for both <i>P. aeruginosa</i> and <i>C. albicans</i>. Choice of metal ion played a crucial role in modulating anti-adhesive activity, with Eu(III) complexes most effective: [Eu·(1Gal)(H<sub>2</sub>O)<sub>6</sub>](CF<sub>3</sub>SO<sub>3</sub>)<sub>3</sub> inhibits 60% biofilm formation by <i>P. aeruginosa</i> and [Eu·(1Gal)<sub>3</sub>](CF<sub>3</sub>SO<sub>3</sub>)<sub>3</sub> inhibits 62% of <i>C. albicans</i> adhesion to buccal epithelial cells (both at 0.1 mM). The results presented demonstrate the potential for metal coordination to significantly enhance biological activity of glycoconjugates, surpassing the effect of the ligand's modest lectin-binding affinity alone.

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Publication Details

Journal
Organic & Biomolecular Chemistry
Published
2025-01-01
DOI
https://doi.org/10.1039/d5ob00970g
Citations
2
Primary Topic
Glycosylation and Glycoproteins Research
Type
article
Field-Weighted Citation Impact
1.61

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article

Antiadhesive glycoconjugate metal complexes targeting pathogens Pseudomonas aeruginosa and Candida albicans

Émilie Gillon, Maria Joyce, Cristina Trujillo, Trinidad Velasco‐Torrijos et al.
2 citations
Organic & Biomolecular Chemistry
Glycosylation and Glycoproteins Research
1.61
article

Antiadhesive glycoconjugate metal complexes targeting pathogens Pseudomonas aeruginosa and Candida albicans

Émilie Gillon, Maria Joyce, Cristina Trujillo, Trinidad Velasco‐Torrijos, Joseph P. Byrne, Karolina Wojtczak, Kevin Kavanagh, Gordon Cooke, Emma Caraher, Anne Imberty, K. M. V. Richmond, Diana Bura, Keela Kessie
article en
2 citations

Abstract

Glycoconjugates are known to interact with carbohydrate-binding proteins involved in adhesion by pathogens, and offer opportunities to design antimicrobial agents. Metal complexes with Eu(III), Ni(II) and Zn(II) were prepared from glycoconjugate ligand 1Gal, which binds to <i>P. aeruginosa</i>'s lectin LecA (<i>K</i><sub>d</sub> 9.6 ± 0.7 μM). <i>In vitro</i> anti-adhesive activity of these compounds was evaluated for both <i>P. aeruginosa</i> and <i>C. albicans</i>. Choice of metal ion played a crucial role in modulating anti-adhesive activity, with Eu(III) complexes most effective: [Eu·(1Gal)(H<sub>2</sub>O)<sub>6</sub>](CF<sub>3</sub>SO<sub>3</sub>)<sub>3</sub> inhibits 60% biofilm formation by <i>P. aeruginosa</i> and [Eu·(1Gal)<sub>3</sub>](CF<sub>3</sub>SO<sub>3</sub>)<sub>3</sub> inhibits 62% of <i>C. albicans</i> adhesion to buccal epithelial cells (both at 0.1 mM). The results presented demonstrate the potential for metal coordination to significantly enhance biological activity of glycoconjugates, surpassing the effect of the ligand's modest lectin-binding affinity alone.

Organic & Biomolecular ChemistryVol. 23(43)
University College Dublin (IE), Centre National de la Recherche Scientifique (FR), National University of Ireland, Maynooth (IE), Ollscoil na Gaillimhe – University of Galway (IE), Trinity College Dublin (IE), University of Manchester (GB), Technological University Dublin (IE), Université Grenoble Alpes (FR)
LABoratoires d’EXcellence ARCANE, European Cooperation in Science and Technology, Science Foundation Ireland, University of Galway, Agence Nationale de la Recherche, Irish Research Council
Openalex Percentile: Top 16%
Glycosylation and Glycoproteins Research
1.61
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