230286-11-0

Basic information

• Product Name: 2-azidoethyl β-D-galactopyranosyl-(1->4)-β-D-glucopyranoside
• Synonyms: 2-azidoethyl β-D-galactopyranosyl-(1->4)-β-D-glucopyranoside
• CAS NO: 230286-11-0
• Molecular Weight: 411.366
• Mol File: 230286-11-0.mol

Chemical Properties

• CAS DataBase Reference: 2-azidoethyl β-D-galactopyranosyl-(1->4)-β-D-glucopyranoside(CAS DataBase Reference)
• NIST Chemistry Reference: 2-azidoethyl β-D-galactopyranosyl-(1->4)-β-D-glucopyranoside(230286-11-0)
• EPA Substance Registry System: 2-azidoethyl β-D-galactopyranosyl-(1->4)-β-D-glucopyranoside(230286-11-0)

Safety Data

• Hazardous Substances Data: 230286-11-0(Hazardous Substances Data)

Usage

Biochem/physiol Actions

2-Azidoethyl β-lactopyranoside is an alkylated glycoside. Alkylated glycosides are used as ligands for Click Chemistry. They may also be important as carbohydrate carriers in glycotherapeutic applications, drug carriers for site-specific delivery, drug enhancers for decreasing toxicity, and solubility and protein enhancers.

Upstream product

• 230286-10-9 2-azidoethyl 2,3,4,6-tetra-O-acetyl-β-lactopyranoside 
• 870136-62-2 2-azidoethyl (2,3,4,6-tetra-O-benzoyl-β-D-galactopyranosyl)-(1->4)-2,3,6-tri-O-benzoyl-β-D-glucopyranoside 
• 499-16-1 lactitol 
• 86651-37-8 2-bromoethyl 4-O-(2,3,4,6-tetra-O-acetyl-β-D-galactopyranosyl)-2,3,6-tri-O-acetyl-β-D-glucopyranoside 
• 5965-66-2 LACTOSE 
• 106256-89-7 (2,3,4,6-tetra-O-acetyl-β-D-galactopyranosyl)-(1->4)-2,3,6-tri-O-acetyl-β-D-glucopyranosyl trichloroacetimidate 
• 92052-38-5 O-<2,3,6-tri-O-acetyl-4-O-(2,3,4,6-tetra-O-acetyl-β-D-galactopyranosyl)-α,β-D-glucopyranosyl>trichloroacetimidate 
• 18464-08-9 2,3,6,2',3',4',6'-hepta-O-acetyl-lactose 
• 70223-97-1 2,3,4,6-tetra-O-acetyl-β-D-galactopyranosyl-(1->4)-2,3,6-tri-O-acetyl-β-D-glucopyranosyl bromide 
• 120232-83-9 2-chloroethyl 2,3,6-tri-O-acetyl-4-O-(2,3,4,6-tetra-O-acetyl-β-D-galactopyranosyl)-β-D-glucopyranoside 
• 4753-07-5 2,3,6,2',3',4',6'-hepta-O-acetyl-lactosyl bromide 
• 18464-08-9 4’-O-(2,3,4,6-tetra-O-acetyl-β-D-galactopyranosyl)-2’,3’,6’-tri-O-acetyl-D-glucopyranose 
• 92052-38-5 2,3,6,2',3',4',6'-hepta-O-acetyl-α-D-lactosyl trichloroacetimidate 
• 61198-91-2 2,3,4,6-tetra-O-benzoyl-β-D-galactopyranosyl-(1→4)-2,3,6-tri-O-benzoyl-α-D-glucopyranosyl bromide 

Downstream Products

• 261155-98-0 2-aminoethyl α-D-galactopyranosyl-(1->4)-β-D-galactopyranosyl-(1->4)-β-D-glucopyranoside 
• 1442748-84-6 (3,4,5)12G₁-PE-spacer-TRZ-(1EO-lactose)₂ 
• 10257-28-0 D-Galactose 
• 165331-08-8 (2R,3R,4S,5S,6R)-2-(2-Azido-ethoxy)-6-hydroxymethyl-tetrahydro-pyran-3,4,5-triol 
• 859838-48-5 aminoethyl 2,3,6-tri-O-benzyl-4-O-(2,3,4,6-tetra-O-benzyl-β-D-galactopyranosyl)-β-D-glucopyranoside 
• 859838-47-4 2-azidoethyl 2,3,6-tri-O-benzyl-4-O-(2,3,4,6-tetra-O-benzyl-β-D-galactopyranosyl)-α-D-glucopyranoside 
• 702686-16-6 2-azidoethyl 4:6-O-phenylmethylene-β-D-galactopyranosyl-(1→4)-β-D-glucopyranoside 
• 503159-47-5 2-azidoethyl 2,6-di-O-benzyl-3-O-p-methoxybenzyl-β-D-galactopyranosyl-(1->4)-2,3,6-tri-O-benzyl-β-D-glucopyranoside 
• 316820-49-2 2-azidoethyl (2,6-O-benzyl-3,4-O-isopropylidene-β-D-galactopyranosyl)-(1->4)-2,3,6-tri-O-benzyl-β-D-glucopyranoside 
• 316820-50-5 2-azidoethyl (2,6-di-O-benzyl-β-D-galactopyranosyl)-(1->4)-2,3,6-tri-O-benzyl-β-D-glucopyranoside 
• 702686-19-9 2-azidoethyl [methyl (5-acetamido-4,7,8,9-tetra-O-acetyl-3,5-dideoxy-D-glycero-α-D-galacto-2-nonulopyranosyl)oate]-(2-> 3)-(2,6-di-O-benzyl-β-D-galactopyranosyl-(1-> 4)-2,3,6-tri-O-benzyl-β-D-glucopyranoside 
• 702686-18-8 2-azidoethyl 2,3,6-tri-O-benzyl-4-O-(2,3-di-O-benzyl-6-O-benzoyl-β-D-galactopyranosyl)-β-D-glucopyranoside 

Relevant articles and documents

Chemoenzymatic synthesis of 2-azidoethyl-ganglio-oligosaccharides GD3, GT3, GM2, GD2, GT2, GM1, and GD1a

We have synthesized several ganglio-oligosaccharide structures using glycosyltransferases from Campylobacter jejuni. The enzymes, α-(2→3/8)-sialyltransferase (Cst-II), β-(1→4)-N- acetylgalactosaminyltransferase (CgtA), and β-(1→3)- galactosyltransferase (CgtB), were produced in large-scale fermentation from Escherichia coli and further characterized based on their acceptor specificities. 2-Azidoethyl-glycosides corresponding to the oligosaccharides of GD3 (α-D-Neup5Ac-(2→8)-α-D-Neup5Ac-(2→3)-β-D-Galp- (1→4)-β-D-Glcp-), GT3 (α-D-Neup5Ac-(2→8)-α-D-Neup5Ac- (2→8)-α-D-Neup5Ac-(2→3)-β-D-Galp-(1→4)-β-D-Glcp-) , GM2 (β-D-GalpNAc-(1→4)-[α-D-Neup5Ac-(2→3)]-β-D-Galp- (1→4)-β-D-Glcp-), GD2 (β-D-GalpNAc-(1→4)-[α-D-Neup5Ac- (2→8)-α-D-Neup5Ac-(2→3)]-β-D-Galp-(1→4) -β-D-Glcp-), GT2 (β-D-GalpNAc-(1→4)-[α-D-Neup5Ac-(2→8) -α-D-Neup5Ac-(2→8)-α-D-Neup5Ac-(2→3)]-β-D-Galp- (1→4)-β-D-Glcp-), and GM1 (β-D-Galp-(1→3)-β-D-GalpNAc- (1→4)-[α-D-Neup5Ac-(2→3)]-β-D-Galp-(1→4) -β-D-Glcp-) were synthesized in high yields (gram-scale). In addition, a mammalian α-(2→3)-sialyltransferase (ST3Gal I) was used to sialylate GM1 and generate GD1a (α-D-Neup5Ac-(2→3)-β-D-Galp-(1→3)- β-D-GalpNAc-(1→4)-[α-D-Neup5Ac-(2→3)]-β-D-Galp- (1→4)-β-D-Glcp-) oligosaccharide. We also cloned and expressed a rat UDP-N-acetylglucosamine-4′epimerase (GalNAcE) in E. coli AD202 cells for cost saving in situ conversion of less expensive UDP-GlcNAc to UDP-GalNAc.

Design and synthesis of cluster neoglycoconjugates based on D-glucose

Synthetic approaches have been developed to tetravalent neoglycoconjugates with different structures of the hydrophobic fragment and D-glucose fragment as branching core. The syntheses have been accomplished by preparation of blocks with terminal C C triple bonds and hydrophobic fragment and hydrophilic component (lactose derivative), followed by their conjugation.

The trans-sialidase from Trypanosoma cruzi efficiently transfers α-(2→3)-linked N-glycolylneuraminic acid to terminal β-galactosyl units

The trans-sialidase from Trypanosoma cruzi (TcTS), the agent of Chagas' disease, is a unique enzyme involved in mammalian host-cell invasion. Since T. cruzi is unable to synthesize sialic acids de novo, TcTS catalyzes the transfer of α-(2→3)-sialyl residues from the glycoconjugates of the host to terminal β-galactopyranosyl units present on the surface of the parasite. TcTS also plays a key role in the immunomodulation of the infected host. Chronic Chagas' disease patients elicit TcTS-neutralizing antibodies that are able to inhibit the enzyme. N-Glycolylneuraminic acid has been detected in T. cruzi, and the trans-sialidase was pointed out as the enzyme involved in its incorporation from host glycoconjugates. However, N-glycolylneuraminic acid α-(2→3)-linked-containing oligosaccharides have not been analyzed as donors in the T. cruzi trans-sialidase reaction. In this paper we studied the ability of TcTS to transfer N-glycolylneuraminic acid from Neu5Gc(α2→3)Gal(β1→4)GlcβOCH2CH2N3 (1) and Neu5Gc(α2→3)Gal(β1→3)GlcNAcβOCH2CH2N3 (2) to lactitol, N-acetyllactosamine and lactose as acceptor substrates. Transfer from 1 was more efficient (50-65%) than from 2 (20-30%) for the three acceptors. The reactions were inhibited when the enzyme was preincubated with a neutralizing antibody. Km values were calculated for 1 and 2 and compared with 3′-sialyllactose using lactitol as acceptor substrate. Analysis was performed by high-performance anion-exchange (HPAEC) chromatography. A competitive transfer reaction of compound 1 in the presence of 3′-sialyllactose and N-acetyllactosamine showed a better transfer of Neu5Gc than of Neu5Ac.

Synthesis of DNP-modified GM3-based anticancer vaccine and evaluation of its immunological activities for cancer immunotherapy

Tumor-associated carbohydrate antigens (TACAs) are attractive targets for vaccine development. In this context, we described a strategy combining artificial TACA and glycoengineering for cancer vaccine development. A 2,4-ditrophenyl (DNP)-modified GM3 int

The design and synthesis of an α-Gal trisaccharide epitope that provides a highly specific anti-Gal immune response

Carbohydrate antigens displaying Galα(1,3)Gal epitopes are recognized by naturally occurring antibodies in humans. These anti-Gal antibodies comprise up to 1% of serum IgG and have been viewed as detrimental as they are responsible for hyperacute organ rejections. In order to model this condition, α(1,3)galactosyltransferase-knockout mice are inoculated against the Galα(1,3)Gal epitope. In our study, two α-Gal trisaccharide epitopes composed of either Galα(1,3)Galβ(1,4)GlcNAc or Galα(1,3)Galβ(1,4)Glc linked to a squaric acid ester moiety were examined for their ability to elicit immune responses in KO mice. Both target epitopes were synthesized using a two-component enzymatic system using modified disaccharide substrates containing a linker moiety for coupling. While both glycoconjugate vaccines induced the required high anti-Gal IgG antibody titers, it was found that this response had exquisite specificity for the Galα(1,3)Galβ(1,4)GlcNAc hapten used, with little cross reactivity with the Galα(1,3)Galβ(1,4)Glc hapten. Our findings indicate that while homogenous glycoconjugate vaccines provide high IgG titers, the carrier and adjuvanting factors can deviate the specificity to an antigenic determinant outside the purview of interest.

Synthesis and antibacterial activities of novel tyrocidine A glycosylated derivatives towards multidrug-resistant pathogens

Glycosylation can have a multifaceted impact on the properties and functions of peptides and plays a critical role in interacting with or binding to the target molecules. Herein, based on the previously reported method for macrocyclic glycopeptide synthesis, two series of tyrocidine A glycosylated derivatives (1a-f and 2a-f) were synthesized and evaluated for their antibacterial activities to further study the structure and activity relationships (SAR). Biological studies showed that the synthetic glycosylated derivatives had good antibacterial activities towards methicillin-resistant Staphylococcus aureus and vancomycin-resistant Enterococcus. SAR studies based on various glycans and linkages were used to enhance the biochemical profile, resulting in the identification of several potent antibiotics, such as 1f, with a great improved therapeutic index than tyrocidine A.

MODULAR SYNTHESIS OF AMPHIPHILIC JANUS GLYCODENDRIMERS AND THEIR SELF-ASSEMBLY INTO GLYCODENDRIMERSOMES

The invention concerns compounds of the formula (I) wherein: Y1 and Y2 are independently a monosaccharide or disaccharide; X1 and X2 are independently -(R9-O)m-, -(R10)P-, -O-(R11-O)q-, -R16-O-R17-O- or a covalent bond; Q1 and Q2 are independently a nitrogen-containing heterocycle moiety; Z1 and Z2 are independently -(O-R7)-, -(O-C(=O)-R8)a-, -O-C(=O)-R12-C(=0)-R13-, -O- C(=O)-R14-C(=O)-R15 or a covalent bond; R7-R17 are each independently C1-C6 alkyl; R1-R6 are each independently a linear or branched alkly group; b, c, d, e, f, and g are 0 or 1, provided b + c + d equals at least 2 and e + f + g equals at least 2; and a, m, p, and q are each an integer from 1-6.

Modular synthesis of amphiphilic Janus glycodendrimers and their self-assembly into glycodendrimersomes and other complex architectures with bioactivity to biomedically relevant lectins

The modular synthesis of 7 libraries containing 51 self-assembling amphiphilic Janus dendrimers with the monosaccharides d-mannose and d-galactose and the disaccharide d-lactose in their hydrophilic part is reported. These unprecedented sugar-containing dendrimers are named amphiphilic Janus glycodendrimers. Their self-assembly by simple injection of THF or ethanol solution into water or buffer and by hydration was analyzed by a combination of methods including dynamic light scattering, confocal microscopy, cryogenic transmission electron microscopy, Fourier transform analysis, and micropipet-aspiration experiments to assess mechanical properties. These libraries revealed a diversity of hard and soft assemblies, including unilamellar spherical, polygonal, and tubular vesicles denoted glycodendrimersomes, aggregates of Janus glycodendrimers and rodlike micelles named glycodendrimer aggregates and glycodendrimermicelles, cubosomes denoted glycodendrimercubosomes, and solid lamellae. These assemblies are stable over time in water and in buffer, exhibit narrow molecular-weight distribution, and display dimensions that are programmable by the concentration of the solution from which they are injected. This study elaborated the molecular principles leading to single-type soft glycodendrimersomes assembled from amphiphilic Janus glycodendrimers. The multivalency of glycodendrimersomes with different sizes and their ligand bioactivity were demonstrated by selective agglutination with a diversity of sugar-binding protein receptors such as the plant lectins concanavalin A and the highly toxic mistletoe Viscum album L. agglutinin, the bacterial lectin PA-IL from Pseudomonas aeruginosa, and, of special biomedical relevance, human adhesion/growth-regulatory galectin-3 and galectin-4. These results demonstrated the candidacy of glycodendrimersomes as new mimics of biological membranes with programmable glycan ligand presentations, as supramolecular lectin blockers, vaccines, and targeted delivery devices.

Site-selective modification of proteins for the synthesis of structurally defined multivalent scaffolds

A combination of classical site-directed mutagenesis, genetic code engineering and bioorthogonal reactions delivered a chemically modified barstar protein with one or four carbohydrates installed at specific residues. These protein conjugates were employed in multivalent binding studies, which support the use of proteins as structurally defined scaffolds for the presentation of multivalent ligands.

Enzymatic synthesis of a 6-sialyl lactose analogue using a pH-responsive water-soluble polymer support

The Letter describes a strategy for the enzymatic synthesis of glycans based on a pH-responsive water-soluble polymer. In neutral condition, the polymer is water-soluble and convenient for in-solution enzymatic synthesis, whereas in acidic condition (pH lower than 4.0), the polymer disconnects with the product and becomes insoluble, which can be easily removed. A 6-Sialyl lactose analogue was synthesized as a model reaction using this approach.