Structure Binding Relationship of ...
Document type :
Article dans une revue scientifique
DOI :
Permalink :
Title :
Structure Binding Relationship of Galactosylated Glycoclusters toward Pseudomonas aeruginosa Lectin LecA Using a DNA-Based Carbohydrate Microarray
Author(s) :
Gerland, Béatrice [Auteur]
Institut des Biomolécules Max Mousseron [Pôle Chimie Balard] [IBMM]
Goudot, Alice [Auteur]
INL - Chimie et Nanobiotechnologies [INL - C&N]
Ligeour, Caroline [Auteur]
Institut des Biomolécules Max Mousseron [Pôle Chimie Balard] [IBMM]
Pourceau, Gwladys [Auteur]
Institut des Biomolécules Max Mousseron [Pôle Chimie Balard] [IBMM]
Meyer, Albert [Auteur]
Institut des Biomolécules Max Mousseron [Pôle Chimie Balard] [IBMM]
Vidal, Sébastien [Auteur]
Institut de Chimie et Biochimie Moléculaires et Supramoléculaires [ICBMS]
Géhin, Thomas [Auteur]
INL - Chimie et Nanobiotechnologies [INL - C&N]
Vidal, Olivier [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 [UGSF]
Souteyrand, Eliane [Auteur]
INL - Chimie et Nanobiotechnologies [INL - C&N]
Vasseur, Jean-Jacques [Auteur]
Institut des Biomolécules Max Mousseron [Pôle Chimie Balard] [IBMM]
Chevolot, Yann [Auteur]
INL - Chimie et Nanobiotechnologies [INL - C&N]
Morvan, François [Auteur]
Institut des Biomolécules Max Mousseron [Pôle Chimie Balard] [IBMM]
Institut des Biomolécules Max Mousseron [Pôle Chimie Balard] [IBMM]
Goudot, Alice [Auteur]
INL - Chimie et Nanobiotechnologies [INL - C&N]
Ligeour, Caroline [Auteur]
Institut des Biomolécules Max Mousseron [Pôle Chimie Balard] [IBMM]
Pourceau, Gwladys [Auteur]
Institut des Biomolécules Max Mousseron [Pôle Chimie Balard] [IBMM]
Meyer, Albert [Auteur]
Institut des Biomolécules Max Mousseron [Pôle Chimie Balard] [IBMM]
Vidal, Sébastien [Auteur]
Institut de Chimie et Biochimie Moléculaires et Supramoléculaires [ICBMS]
Géhin, Thomas [Auteur]
INL - Chimie et Nanobiotechnologies [INL - C&N]
Vidal, Olivier [Auteur]

Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 [UGSF]
Souteyrand, Eliane [Auteur]
INL - Chimie et Nanobiotechnologies [INL - C&N]
Vasseur, Jean-Jacques [Auteur]
Institut des Biomolécules Max Mousseron [Pôle Chimie Balard] [IBMM]
Chevolot, Yann [Auteur]
INL - Chimie et Nanobiotechnologies [INL - C&N]
Morvan, François [Auteur]
Institut des Biomolécules Max Mousseron [Pôle Chimie Balard] [IBMM]
Journal title :
Bioconjugate chemistry
Volume number :
25
Pages :
379-392
Publication date :
2014-02-19
ISSN :
1043-1802, 1520-4812
English keyword(s) :
Peptides
Proteins
Fluorescence
Scaffolds
Aromatic compounds
Cluster chemistry
Proteins
Fluorescence
Scaffolds
Aromatic compounds
Cluster chemistry
HAL domain(s) :
Chimie/Chimie théorique et/ou physique
English abstract : [en]
Pseudomonas aeruginosa (PA) is a major public health issue due to its impact on nosocomial infections as well as its impact on cystic fibrosis patient mortality. One of the main concerns is its ability to develop antibiotic ...
Show more >Pseudomonas aeruginosa (PA) is a major public health issue due to its impact on nosocomial infections as well as its impact on cystic fibrosis patient mortality. One of the main concerns is its ability to develop antibiotic resistance. Therefore, inhibition of PA virulence has been proposed as an alternative strategy to tackle PA based infections. LecA (or PA-IL), a galactose binding lectin from PA, is involved in its virulence. Herein, we aimed at designing high affinity synthetic ligands toward LecA for its inhibition and at understanding the key parameters governing the binding of multivalent galactosylated clusters. Twenty-five glycoclusters were synthesized and their bindings were studied on a carbohydrate microarray. Monosaccharide centered clusters and linear comb-like clusters were synthesized with different linkers separating the core and the galactosyl residues. Their length, flexibility, and aromaticity were varied. Our results showed that the binding profile of LecA to galactosylated clusters was dependent on both the core and the linker and also that the optimal linker was different for each core. Nevertheless, an aryl group in the linker structure drastically improved the binding to LecA. Our results also suggest that optimal distances are preferred between the core and the aromatic group and the core and the galactose.Show less >
Show more >Pseudomonas aeruginosa (PA) is a major public health issue due to its impact on nosocomial infections as well as its impact on cystic fibrosis patient mortality. One of the main concerns is its ability to develop antibiotic resistance. Therefore, inhibition of PA virulence has been proposed as an alternative strategy to tackle PA based infections. LecA (or PA-IL), a galactose binding lectin from PA, is involved in its virulence. Herein, we aimed at designing high affinity synthetic ligands toward LecA for its inhibition and at understanding the key parameters governing the binding of multivalent galactosylated clusters. Twenty-five glycoclusters were synthesized and their bindings were studied on a carbohydrate microarray. Monosaccharide centered clusters and linear comb-like clusters were synthesized with different linkers separating the core and the galactosyl residues. Their length, flexibility, and aromaticity were varied. Our results showed that the binding profile of LecA to galactosylated clusters was dependent on both the core and the linker and also that the optimal linker was different for each core. Nevertheless, an aryl group in the linker structure drastically improved the binding to LecA. Our results also suggest that optimal distances are preferred between the core and the aromatic group and the core and the galactose.Show less >
Language :
Anglais
Audience :
Non spécifiée
Administrative institution(s) :
CNRS
Université de Lille
Université de Lille
Research team(s) :
Génétique des enveloppes bactériennes
Submission date :
2020-02-12T15:44:37Z
2021-04-22T08:53:33Z
2021-04-22T08:53:33Z