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Characterization of the interaction of multivalent glycosylated ligands with bacterial lectins by biolayer interferometry.

Léo PicaultEugénie LaigreEmilie GillonClaire TiertantOlivier RenaudetAnne ImbertyDavid GoyardJérôme Dejeu
Published in: Glycobiology (2022)
The study of multivalent carbohydrate-protein interactions remains highly complicated and sometimes rendered impossible due to aggregation problems. Biolayer interferometry is emerging as a tool to monitor such complex interactions. In this study, various glycoclusters and dendrimers were prepared and evaluated as ligands for lectins produced by pathogenic bacteria Pseudomonas aeruginosa (LecA and Lec B) and Burkholderia ambifaria (BambL). Reliable kinetic and thermodynamic parameters could be measured, and immobilization of either lectin or ligands resulted in high quality data. The methods gave results in full agreement with previous isothermal titration calorimetry experiments, and presented strong advantages because they require less quantity and purity for the biomolecules.
Keyphrases
  • pseudomonas aeruginosa
  • cystic fibrosis
  • high speed
  • mass spectrometry
  • small molecule
  • high resolution
  • biofilm formation
  • multidrug resistant
  • staphylococcus aureus
  • deep learning
  • acinetobacter baumannii