The assessment of binding of divalent galactosides for LecA inhibition
Pseudomonas aeruginosa is a widespread opportunistic pathogen that is capable of colonizing various human tissues and that is resistant to many antibiotics. LecA is a galactose binding tetrameric lectin involved in adhesion, infection and biofilm formation. This poster briefly reports the binding characteristics of LecA to mono- and divalent ligands using different techniques. These include Affinity Capillary Electrophoresis, Bio Layer Interferometry, Native Mass Spectrometry, Isothermal Titration Calorimetry and a Thermal Shift Assay. Aspects of focus include affinity, selectivity and binding kinetics.
