AI Article Synopsis
- LecA from Pseudomonas aeruginosa is a key virulence factor, making it a target for potential treatments against infections caused by this bacterium.
- Researchers have designed 32 glycodendrimers with a specific structure aimed at effectively binding to LecA and competing with human glycoconjugates.
- The binding affinity of these glycodendrimers was tested using microarray techniques, resulting in high-affinity compounds with low nanomolar binding values, indicating strong potential for therapeutic use.
Article Abstract
Lectin A (LecA) from Pseudomonas aeruginosa is an established virulence factor. Glycoclusters that target LecA and are able to compete with human glycoconjugates present on epithelial cells are promising candidates to treat P. aeruginosa infection. A family of 32 glycodendrimers of generation 0 and 1 based on a bifurcated bis-galactoside motif have been designed to interact with LecA. The influences both of the central multivalent core and of the aglycon of these glycodendrimers on their affinity toward LecA have been evaluated by use of a microarray technique, both qualitatively for rapid screening of the binding properties and also quantitatively (K ). This has led to high-affinity LecA ligands with K values in the low nanomolar range (K =22 nm for the best one).
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| http://dx.doi.org/10.1002/cbic.201700154 | DOI Listing |
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