Molecular recognition of glycans plays an important role in glycomic and glycobiology studies. For example, pathogens have a number of different types of lectin for targeting host sugars. In bacteria, lectins exist sometimes as domains of bacterial toxins and exploit adhesion to glycoconjugates as a means of entering host cells. Herein, we describe the synthesis of three glycodendrons with the aim to dissect the fine structural details involved in the multivalent carbohydrate-protein interactions. LecA, from the pathogen Pseudomonas aeruginosa, has been used to characterize galactose dendrons interaction using one of the most widespread NMR technique for the elucidation of receptor-ligand binding in solution, the saturation transfer difference (STD) NMR. Furthermore, the effective hydrodynamic radius of each dendrimer recognized by LecA was estimated from the diffusion coefficients determined by pulsed-field-gradient stimulated echo (PFG-STE) NMR experiments.

Bini, D., Marchetti, R., Russo, L., Molinaro, A., Silipo, A., & Cipolla, L. (2016). Multivalent ligand mimetics of LecA from P. aeruginosa: Synthesis and NMR studies. CARBOHYDRATE RESEARCH, 429, 23-28 [10.1016/j.carres.2016.04.023].

Multivalent ligand mimetics of LecA from P. aeruginosa: Synthesis and NMR studies

BINI, DAVIDE
Primo
;
RUSSO, LAURA;CIPOLLA, LAURA FRANCESCA
2016

Abstract

Molecular recognition of glycans plays an important role in glycomic and glycobiology studies. For example, pathogens have a number of different types of lectin for targeting host sugars. In bacteria, lectins exist sometimes as domains of bacterial toxins and exploit adhesion to glycoconjugates as a means of entering host cells. Herein, we describe the synthesis of three glycodendrons with the aim to dissect the fine structural details involved in the multivalent carbohydrate-protein interactions. LecA, from the pathogen Pseudomonas aeruginosa, has been used to characterize galactose dendrons interaction using one of the most widespread NMR technique for the elucidation of receptor-ligand binding in solution, the saturation transfer difference (STD) NMR. Furthermore, the effective hydrodynamic radius of each dendrimer recognized by LecA was estimated from the diffusion coefficients determined by pulsed-field-gradient stimulated echo (PFG-STE) NMR experiments.
Articolo in rivista - Articolo scientifico
Dendrons; Lectins; Ligand mimetics; P. aeruginosa; PFG-STE NMR experiments; STD NMR;
Dendrons; Lectins; Ligand mimetics; P. aeruginosa; PFG-STE NMR experiments; STD NMR; Analytical Chemistry; Biochemistry; Organic Chemistry
English
23
28
6
Bini, D., Marchetti, R., Russo, L., Molinaro, A., Silipo, A., & Cipolla, L. (2016). Multivalent ligand mimetics of LecA from P. aeruginosa: Synthesis and NMR studies. CARBOHYDRATE RESEARCH, 429, 23-28 [10.1016/j.carres.2016.04.023].
Bini, D; Marchetti, R; Russo, L; Molinaro, A; Silipo, A; Cipolla, L
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/10281/135147
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