Monovalent and bivalent N-fucosyl amides as high affinity ligands for Pseudomonas aeruginosa PA-IIL lectin.
The adhesion of bacteria to human glycoconjugates can be inhibited by soluble glycomimetics that compete with the natural target. Four monovalent and one divalent alpha-fucosyl amides have been tested for their affinity for a fucose-binding lectin from Pseudomonas aeruginosa. Isothermal calorimetric titrations demonstrated that they bind to the lectin in the micromolar range, with highest affinity for the divalent ligand. Molecular modelling established that, compared to Omicron-fucoside compounds, the glycomimetic amide group resulted in the loss of water-bridged hydrogen bonds that could be partially compensated by additional contact of the aglycone with the protein surface.
Andreini
Manuel
M
Universita' degli Studi di Milano, Dipartimento di Chimica Organica e Industriale, via Venezian 21, I-20133 Milano, Italy.
Anderluh
Marko
M
Audfray
Aymeric
A
Bernardi
Anna
A
Imberty
Anne
A
D018829:Adhesins, Bacterial / Q000737:chemistry / Q000378:metabolism*; D000577:Amides / Q000737:chemistry*; D005643:Fucose / Q000737:chemistry* / Q000378:metabolism*; D006031:Glycosylation; D037102:Lectins / Q000737:chemistry / Q000378:metabolism*; D008024:Ligands; D008958:Models, Molecular; D011485:Protein Binding; D011487:Protein Conformation; D011550:Pseudomonas aeruginosa
D018829:Adhesins, Bacterial; D000577:Amides; D037102:Lectins; D008024:Ligands; C038692:adhesin, Pseudomonas; D005643:Fucose