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Design and Synthesis of Galactosylated Bifurcated Ligands with Nanomolar Affinity for Lectin LecA from Pseudomonas aeruginosa
Author(s) -
Angeli Anthony,
Li Muchen,
Dupin Lucie,
Vergoten Gérard,
Noël Mathieu,
Madaoui Mimouna,
Wang Shuai,
Meyer Albert,
Géhin Thomas,
Vidal Sébastien,
Vasseur JeanJacques,
Chevolot Yann,
Morvan François
Publication year - 2017
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201700154
Subject(s) - glycoconjugate , pseudomonas aeruginosa , lectin , chemistry , virulence factor , virulence , glycoprotein , microbiology and biotechnology , biochemistry , combinatorial chemistry , bacteria , biology , genetics , gene
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 d ). This has led to high‐affinity LecA ligands with K d values in the low nanomolar range ( K d =22 n m for the best one).