Conformational Differences Between C- and O-Glycosides: The -C-Mannobiose/-O-Mannobiose Case

Espinosa, Juan F.; Bruix, Marta; Jarreton, Olivier; Skrydstrup, Troels; Beau, Jean‐Marie; Jiménez‐Barbero, Jesús

doi:10.1002/(sici)1521-3765(19990201)5:2<442::aid-chem442>3.3.co;2-t

Cited by 19 publications

(29 citation statements)

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“…Next, the conformation around the glycosidic linkage was assessed through NOE experiments. Only the expected interresidue GalH1 to GlcH4 (overlapping with GlcH3) and GlcH6 NOEs were observed indicating that LacDP adopts the natural exo-anomeric syn-ΦΨ geometry of lactose around the glycosidic linkage [52]. No intramolecular aromatic-sugar NOEs were observed, indicating that no stacking of the aromatic moiety onto the sugar faces takes place.…”

Section: Synthesis Of Biotinylated Fluorescent Glycoconjugatementioning

confidence: 98%

Versatile strategy for the synthesis of biotin-labelled glycans, their immobilization to establish a bioactive surface and interaction studies with a lectin on a biochip

et al. 2008

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The emerging role of glycans as versatile biochemical signals in diverse aspects of cellular sociology calls for establishment of sensitive methods to monitor carbohydrate recognition by receptors such as lectins. Most of these techniques involve the immobilization of one of the binding partners on a surface, e.g. atomic force microscopy, glycan array and Surface Plasmon Resonance (SPR), hereby simulating cell surface presentation. Here, we report the synthesis of fluorescent glycoconjugates, with a functionalization strategy which avoids the frequently occurring ring opening at the reducing end for further immobilization on a surface or derivatization with biotin. In order to improve the versatility of these derivatized glycans for biological studies, a new approach for the synthesis of biotinylated and fluorescent glycans has also been realized. Finally, to illustrate their usefulness the neoglycoconjugates were immobilized on different surfaces, and the interaction analysis with a model lectin, the toxin from mistletoe, proved them to act as potent ligands, underscoring the merit of the presented synthetic approach.

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Section: Synthesis Of Biotinylated Fluorescent Glycoconjugatementioning

confidence: 98%

Versatile strategy for the synthesis of biotin-labelled glycans, their immobilization to establish a bioactive surface and interaction studies with a lectin on a biochip

et al. 2008

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“…3 Indeed, C-mannobiose presents significant differences relative to its parent O-glycoside. 4 These findings have encouraged us to extend the comparison between C-and O-glycosides to other pairs. Along these lines, we now report the conformational analysis of the C-disaccharide b-C-Gal-(1!4)-bGlcNAc-OMe 5 (1) in water using NMR spectroscopy assisted by molecular mechanics calculations, and a comparison with the parent O-disaccharide (2).…”

Section: Introductionmentioning

confidence: 99%

The conformation of the C-glycosyl analogue of N-acetyl-lactosamine in the free state and bound to a toxic plant agglutinin and human adhesion/growth-regulatory galectin-1

Garcı́a-Aparicio

Sollogoub

Blériot

et al. 2007

Carbohydrate Research

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“…Although still debatable whether C-glycosides possess similar conformations as their parent O-glycosides [38][39][40][41][42][43][44][45][46], it has been known that the C-glycosides may mimic the parent O-glycosides in lectin and other ligand-binding activities [38,44,[47][48][49]. Because of their ability to resist enzymatic hydrolysis, C-glycoside inhibitors were designed and synthesized as substrate mimics for both glycosidases and glycosyltransferases.…”

Section: C-glycoside Based Inhibitorsmentioning

confidence: 99%

C-Glycosides and Aza-C-Glycosides as Potential Glycosidase and Glycosyltransferase Inhibitors

Zou¹

2005

CTMC

146

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Glycosylation as one of most important post-translational modification of gene products is often critical to specific cellular biological functions. Since elevated glycoprocessing enzyme activities have been implicated in the development of various diseases including cancer metastasis, glycosidases and glycosyltransferases are considered as therapeutic targets. Azasugars, the first generation of enzyme inhibitors, have been extensively investigated and two azasugar-based drugs (Miglitol and Miglustat) have been approved. Aza-C-glycosides, molecules with an azasugar core and various C-aglycons attached at the pseudo anomeric center, have the potential to become the second-generation inhibitors with improved specificity and membrane permeability. In this review, C-glycosides, aza-C-glycosides, and aza-C-disaccharides are introduced as glycoprocessing enzyme inhibitors. The synthetic approaches toward those molecules are described based on the key reactions, which include reductive amination, nucleophilic ring opening of epoxides, nucleophilic addition to imines (C=N), and hetero-Michael additions. Aza-C-glycoside-based libraries are also described for the discovery of promising second-generation inhibitors.

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Conformational Differences Between C- and O-Glycosides: The -C-Mannobiose/-O-Mannobiose Case

Cited by 19 publications

References 0 publications

Versatile strategy for the synthesis of biotin-labelled glycans, their immobilization to establish a bioactive surface and interaction studies with a lectin on a biochip

Versatile strategy for the synthesis of biotin-labelled glycans, their immobilization to establish a bioactive surface and interaction studies with a lectin on a biochip

The conformation of the C-glycosyl analogue of N-acetyl-lactosamine in the free state and bound to a toxic plant agglutinin and human adhesion/growth-regulatory galectin-1

C-Glycosides and Aza-C-Glycosides as Potential Glycosidase and Glycosyltransferase Inhibitors

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