Probing β-(1→3)-d-glucans interactions with recombinant human receptors using high-resolution NMR studies

Sylla, Balla; Guégan, Jean‐Paul; Wieruszeski, Jean‐Michel; Nugier‐Chauvin, Caroline; Legentil, Laurent; Daniellou, Richard; Ferrières, Vincent

doi:10.1016/j.carres.2011.03.038

Cited by 26 publications

(33 citation statements)

References 27 publications

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“…Bose’s team showed that soluble β-glucans of 10 kDa could bind human neutrophils and monocytes in a concentration-dependent and receptor-specific manner [51]. It was also proposed, and confirmed later with STD-NMR studies [31], that small soluble oligosaccharides (less than 10 repeating units) cannot bind the lectin site [30]. More recently, Crich and coworkers analyzed the effects of shorter hydroxylamine analogues of β-glucan.…”

Section: Interactions Of β-(1→3)-glucans With Human Main Receptorsmentioning

confidence: 99%

“…Such a NMR sequence is able to give a dynamic view of the contacts between a small molecule and its macromolecular receptor in solution. On this basis, it was established that Dectin-1 induced less contacts with H-2 and H-4 than with H-3, H-5, H-6 and anomeric H-1 [31]. This means that interactions occurred between the hydrophobic face of the glucan and hydrophobic groove of the lectin site through amino acid residues such as histidine and more particularly tryptophan.…”

Section: Interactions Of β-(1→3)-glucans With Human Main Receptorsmentioning

confidence: 99%

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Molecular Interactions of β-(1→3)-Glucans with Their Receptors

et al. 2015

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β-(1→3)-Glucans can be found as structural polysaccharides in cereals, in algae or as exo-polysaccharides secreted on the surfaces of mushrooms or fungi. Research has now established that β-(1→3)-glucans can trigger different immune responses and act as efficient immunostimulating agents. They constitute prevalent sources of carbons for microorganisms after subsequent recognition by digesting enzymes. Nevertheless, mechanisms associated with both roles are not yet clearly understood. This review focuses on the variety of elucidated molecular interactions that involve these natural or synthetic polysaccharides and their receptors, i.e., Dectin-1, CR3, glycolipids, langerin and carbohydrate-binding modules.

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Section: Interactions Of β-(1→3)-glucans With Human Main Receptorsmentioning

confidence: 99%

Section: Interactions Of β-(1→3)-glucans With Human Main Receptorsmentioning

confidence: 99%

Molecular Interactions of β-(1→3)-Glucans with Their Receptors

et al. 2015

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“…As such, the NMR investigation of these interactions remains an important technical and methodological challenge. Different STD NMR studies confirmed that the binding affinity of β‐glucans to Dectin‐1 depends on the number of repeating units; this is also confirmed by other biophysical techniques. Laminarihexose, for instance, showed very weak or no STD response, whereas Laminarin (18 to 31 units) provided clear STD signals.…”

Section: Applicationsmentioning

confidence: 99%

“Rules of Engagement” of Protein-Glycoconjugate Interactions: A Molecular View Achievable by using NMR Spectroscopy and Molecular Modeling

et al. 2016

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Understanding the dynamics of protein–ligand interactions, which lie at the heart of host–pathogen recognition, represents a crucial step to clarify the molecular determinants implicated in binding events, as well as to optimize the design of new molecules with therapeutic aims. Over the last decade, advances in complementary biophysical and spectroscopic methods permitted us to deeply dissect the fine structural details of biologically relevant molecular recognition processes with high resolution. This Review focuses on the development and use of modern nuclear magnetic resonance (NMR) techniques to dissect binding events. These spectroscopic methods, complementing X‐ray crystallography and molecular modeling methodologies, will be taken into account as indispensable tools to provide a complete picture of protein–glycoconjugate binding mechanisms related to biomedicine applications against infectious diseases.

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“…The related hydroxylamine analogues ( 2 ) were also synthesized and showed comparable affinity to the 5-thiopyranosyl derivatives [75,76]. The di-and tri-hydroxylamine mimetics were both shown to inhibit CR3 and dectin-1 binding, which was again attributed to the increase in hydrophobic nature resulting from the more polarizable hydroxylamine moiety and lack of a C-2 substituent [76,77,78], which could then interact more strongly with hydrophobic residues in the binding site (e.g., Trp221 and His223 in dectin-1 [79]).…”

Section: Replacement Of the Endocyclic O Atommentioning

confidence: 99%

Bioisosteres of Carbohydrate Functional Groups in Glycomimetic Design

Hevey

2019

Biomimetics

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The aberrant presentation of carbohydrates has been linked to a number of diseases, such as cancer metastasis and immune dysregulation. These altered glycan structures represent a target for novel therapies by modulating their associated interactions with neighboring cells and molecules. Although these interactions are highly specific, native carbohydrates are characterized by very low affinities and inherently poor pharmacokinetic properties. Glycomimetic compounds, which mimic the structure and function of native glycans, have been successful in producing molecules with improved pharmacokinetic (PK) and pharmacodynamic (PD) features. Several strategies have been developed for glycomimetic design such as ligand pre-organization or reducing polar surface area. A related approach to developing glycomimetics relies on the bioisosteric replacement of carbohydrate functional groups. These changes can offer improvements to both binding affinity (e.g., reduced desolvation costs, enhanced metal chelation) and pharmacokinetic parameters (e.g., improved oral bioavailability). Several examples of bioisosteric modifications to carbohydrates have been reported; this review aims to consolidate them and presents different possibilities for enhancing core interactions in glycomimetics.

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Probing β-(1→3)-d-glucans interactions with recombinant human receptors using high-resolution NMR studies

Cited by 26 publications

References 27 publications

Molecular Interactions of β-(1→3)-Glucans with Their Receptors

Molecular Interactions of β-(1→3)-Glucans with Their Receptors

“Rules of Engagement” of Protein-Glycoconjugate Interactions: A Molecular View Achievable by using NMR Spectroscopy and Molecular Modeling

Bioisosteres of Carbohydrate Functional Groups in Glycomimetic Design

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