773896-71-2

Upstream product

• 532-20-7 D-Ribose 
• 107-18-6 allyl alcohol 
• 2280-44-6 D-Glucose 
• 50-69-1 D-ribose 
• 532-20-7 L-arabinose 
• 22796-65-2 p-nitrophenyl α-L-arabinofuranoside 
• 58-86-6 D-xylose 
• 28697-53-2 D-arabinopyranose 
• 106-95-6 allyl bromide 
• 10323-20-3 D-Arabinose 
• 532-20-7 D-arabinofuranose 
• 532-20-7 D-lyxose 
• 41546-31-0 L-xylose 
• 1949-78-6 L-lyxose 

Downstream Products

• 121682-55-1 allyl 2,3,5-tri-O-benzyl-α,β-D-ribofuranoside 
• 67814-68-0 2,3-O-isopropylidene-D-ribofuranose 
• 121682-55-1 allyl-2,3,5-tri-O-benzyl-α,β-L-arabinofuranoside 
• 1431388-85-0 N-acetyl-2,3-aziridino-5-O-benzoyl-2,3-dideoxy-d-ribofuranose 
• 1431388-86-1 N-acetyl-2,3-aziridino-5-O-benzoyl-2,3-dideoxy-d-ribofuranose 

Relevant academic research and scientific papers

Anomeric alkylations and acylations of unprotected mono- and disaccharides mediated by pyridoneimine in aqueous solutions

A site-specific deprotonation followed by alkylations and acylations of sugar hemiacetals to the corresponding alkyl glycosides and acylated sugars in aqueous solutions is disclosed herein. Pyridoneimine as a new base is developed to mediate the deprotonation of readily available sugar hemiacetals and further reactions with alkylation and acylation agents.

Synthesis of Phenolic Glycosides: Glycosylation of Sugar Lactols with Aryl Bromides via Dual Photoredox/Ni Catalysis

Multifarious sugar lactols were efficiently transformed into the corresponding phenolic glycosides by treating with aryl bromides in acetonitrile with Ir[dF(CF3)ppy]2(dtbbpy)(PF6) as a photocatalyst under visible light irr

Expedient Synthesis of a Linear Nonadecaarabinofuranoside of the Mycobacterium tuberculosis Cellular Envelope

The synthesis of oligosaccharides is demanding as it requires multiple steps and long reaction sequences. The choice of glycosylation method and protecting groups is very important for the successful synthesis of any oligosaccharide. In this paper, we show that ethynylcyclohexyl carbonate glycosyl donors are excellent for the synthesis of a nonadecasaccharide fragment of the Mycobacterium tuberculosis glycocalyx using a split/react/couple strategy. The synthesis of the target nonadecasaccharide was accomplished using eight different reactions and 23 steps in 6.4 % overall yield.

Analysis of Configuration and Conformation of Furanose Ring in Carbohydrate and Nucleoside by Vibrational Circular Dichroism

A reliable and convenient method for determining the configuration and conformation of the furanose ring in carbohydrates and nucleosides by vibrational circular dichroism (VCD) spectroscopy is described. Diastereomeric pairs of several furanose monosacch

Synthesis and Macrodomain Binding of Mono-ADP-Ribosylated Peptides

Mono-ADP-ribosylation is a dynamic posttranslational modification (PTM) with important roles in signaling. Mammalian proteins that recognize or hydrolyze mono-ADP-ribosylated proteins have been described. We report the synthesis of ADP-ribosylated peptides from the proteins histone H2B, RhoA and, HNP-1. An innovative procedure was applied that makes use of pre-phosphorylated amino acid building blocks. Binding assays revealed that the macrodomains of human MacroD2 and TARG1 exhibit distinct specificities for the different ADP-ribosylated peptides, thus showing that the sequence surrounding ADP-ribosylated residues affects the substrate selectivity of macrodomains.

Sulfonated graphene oxide as highly efficient catalyst for glycosylation

Heterogeneous sulfonated graphene oxide for the first time has been used as a green and efficient catalyst for atom-economic glycosylation of unprotected, unactivated glycosyl donors or 2,3,4,6-tetra-O-acetylglycosyltrichloroacetimidate with various accep

Araf51 with improved transglycosylation activities: One engineered biocatalyst for one specific acceptor

A random mutagenesis of the arabinofuranosyl hydrolase Araf51 has been run in order to have access to efficient biocatalysts for the synthesis of alkyl arabinofuranosides. The mutants were selected on their ability to catalyze the transglycosylation reaction of p-nitrophenyl α-l-arabinofuranoside (pNP-Araf) used as a donor and various aliphatic alcohols as acceptors. This screening strategy underlined 5 interesting clones, each one corresponding to one acceptor. They appeared to be much more efficient in the transglycosylation reaction compared to the wild type enzyme whereas no self-condensation or hydrolysis products could be detected. Moreover, the high specificity of the mutants toward the alcohols for which they have been selected validates the screening process. Sequence analysis of the mutated enzymes revealed that, despite their location far from the active site, the mutations affect significantly the kinetics properties as well as the substrate affinity of these mutants toward the alcohol acceptors in the transglycosylation reaction.

Synthesis of the spirastrellolide A, B/C spiroketal: Enabling solutions for problematic au(I)-catalyzed spiroketalizations

A synthesis of the spirastrellolide A, B/C-ring monounsaturated spiroketal is reported. The key step relies on a Au-catalyzed spiroketalization of a propargyl triol employing an acetonide as a regioselectivity regulator. Through observation and analysis, a set of conditions has been developed that facilitates the use of a mixture of diastereomeric substrates, obviating the need to control the stereochemistry of the propargyl stereocenter and enabling a convenient retrosynthetic disconnection. The key reaction proceeds in 80% yield in 1 min at ambient temperature with the Me3PAuCl/AgOTf catalyst system. These conditions should be widely applicable for new synthetic endeavors as they appear to overcome all issues with the Au-catalyzed spiroketalization.

Araf51 with improved transglycosylation activities: One engineered biocatalyst for one specific acceptor

A random mutagenesis of the arabinofuranosyl hydrolase Araf51 has been run in order to have access to efficient biocatalysts for the synthesis of alkyl arabinofuranosides. The mutants were selected on their ability to catalyze the transglycosylation reaction of p-nitrophenyl α-l-arabinofuranoside (pNP-Araf) used as a donor and various aliphatic alcohols as acceptors. This screening strategy underlined 5 interesting clones, each one corresponding to one acceptor. They appeared to be much more efficient in the transglycosylation reaction compared to the wild type enzyme whereas no self-condensation or hydrolysis products could be detected. Moreover, the high specificity of the mutants toward the alcohols for which they have been selected validates the screening process. Sequence analysis of the mutated enzymes revealed that, despite their location far from the active site, the mutations affect significantly the kinetics properties as well as the substrate affinity of these mutants toward the alcohol acceptors in the transglycosylation reaction.

Stereoselective ribosylation of amino acids

The glycosylation properties of ribofuranosyl N-phenyltrifluoroacetimidates toward carboxamide side chains of asparagine and glutamine were investigated. Conditions were found that promote nearly exclusive formation of the α-anomerically configured N-glycosides. The strategy allows for the synthesis of Fmoc-amino acids suitably modified for the preparation of ADP-ribosylated peptides. Furthermore, ribosylation of serine with these donors proved to be completely α-selective, and for the first time, α-ribosylated glutamic and aspartic acid, the naturally occurring sites for poly-ADP-ribosylation, were synthesized.