48149-72-0

Usage

Uses

Used in Pharmaceutical Industry:
ALLYL ALPHA-D-GALACTOPYRANOSIDE is used as a synthetic intermediate for the production of oligosaccharides, which are crucial in the development of various pharmaceutical compounds. These oligosaccharides play a vital role in cell recognition, cell adhesion, and signal transduction, making them essential for the development of drugs targeting these biological processes.
Used in Chemical Industry:
In the chemical industry, ALLYL ALPHA-D-GALACTOPYRANOSIDE is utilized as a synthetic intermediate for the synthesis of complex carbohydrate structures. These structures are vital in various applications, such as the development of new materials, catalysts, and sensors, as well as in the study of carbohydrate chemistry and biochemistry.
Used in Research and Development:
ALLYL ALPHA-D-GALACTOPYRANOSIDE is also used in research and development for the study of carbohydrate-based compounds and their potential applications in various fields. This includes the development of new drugs, the study of carbohydrate interactions with proteins and other biomolecules, and the exploration of novel synthetic methods for the preparation of complex carbohydrate structures.

InChI:InChI=1/C9H16O6/c1-2-3-14-9-8(13)7(12)6(11)5(4-10)15-9/h2,5-13H,1,3-4H2/t5?,6-,7-,8?,9-/m0/s1

Upstream product

• 59-23-4 D-Galactose 
• 107-18-6 allyl alcohol 
• 40733-07-1 D-Galactose-dibenzyldithioacetal 
• 10257-28-0 D-Galactose 
• 512-69-6 D-raffinose 
• 1190202-85-7 but-2-yn-1-yl β-D-galactopyranoside 
• 151168-59-1 1-propynyl-β-D-galactopyranoside 
• 2595-07-5 allyl D-galactopyranoside 
• 28244-97-5 phenyl-1-thio-α-D-galactopyranoside 
• 28512-68-7 phenyl 2,3,4,6-tetra-O-acetyl-1-thio-α-D-galactopyranoside 
• 25878-60-8 D-galactose pentaacetate 
• 3646-73-9 α-D-galactopyranose 
• 106-95-6 allyl bromide 
• 2280-44-6 D-Glucose 

Downstream Products

• 20746-64-9 allyl 4,6-O-benzylidene-α-D-galactopyranoside 
• 258854-17-0 1-O-Allyl 6-O-trityl-α-D-galactopyranoside 
• 183954-75-8 allyl 3-O-<(p-methoxyphenyl)methyl>-α-D-galactopyranoside 
• 61893-74-1 allyl 2,3,6-tri-O-benzyl-α-D-galactopyranoside 
• 918334-10-8 2,3-di-O-benzyl-4,6-O-di-tert-butylsilylene-α-D-galactopyranose 
• 918334-09-5 allyl 2,3-di-O-benzyl-4,6-O-di-tert-butylsilylene-α-D-galactopyranoside 
• 918334-11-9 O-(2,3-di-O-benzyl-4,6-O-di-tert-butylsilylene-α-D-galactopyranosyl) trichloroacetimidate 
• 918334-17-5 (2S,3S,4R)-2-amino-3,4-bis(benzyloxy)-1-(2,3-di-O-benzyl-4,6-O-di-tert-butylsilylene-α-D-galactopyranosyloxy)nonane 
• 195316-89-3 allyl 2,3,4-tri-O-benzoyl-α-D-galactopyranoside 
• 195316-91-7 allyl 2,3,4-tri-O-benzoyl-6-O-trimethylsilyl-α-D-galactopyranoside 

Relevant academic research and scientific papers

A facile synthesis of per-O-alkylated glycono-δ-lactones from per-O-alkylated glycopyranosides and a novel ring contraction for pyranoses

A novel one-pot synthesis of a variety of O-peralkylated δ-aldonolactones 9 from their corresponding glycosides 1 is introduced. This facile procedure involves combining glycoside precursor, tin(IV) chloride and trimethylsilyl azide in methylene chloride

Photorhabdus luminescens lectin A (PllA): A new probe for detecting -galactoside–terminating glycoconjugates

Lectins play important roles in infections by pathogenic bacteria, for example, in host colonization, persistence, and biofilm formation. The Gram-negative entomopathogenic bacterium Photorhabdus luminescens symbiotically lives in insect-infecting Heterorhabditis nematodes and kills the insect host upon invasion by the nematode. The P. luminescens genome harbors the gene plu2096, coding for a novel lectin that we named PllA. We analyzed the binding properties of purified PllA with a glycan array and a binding assay in solution. Both assays revealed a strict specificity of PllA for -galactoside–terminating glycoconjugates. The crystal structures of apo PllA and complexes with three different ligands revealed the molecular basis for the strict specificity of this lectin. Furthermore, we found that a 90° twist in subunit orientation leads to a peculiar quaternary structure compared with that of its ortholog LecA from Pseudomonas aeruginosa. We also investigated the utility of PllA as a probe for detecting -galactosides. The -Gal epitope is present on wild-type pig cells and is the main reason for hyperacute organ rejection in pig to primate xenotransplantation. We noted that PllA specifically recognizes this epitope on the glycan array and demonstrated that PllA can be used as a fluorescent probe to detect this epitope on primary porcine cells in vitro. In summary, our biochemical and structural analyses of the P. luminescens lectin PllA have disclosed the structural basis for PllA’s high specificity for -galactoside–containing ligands, and we show that PllA can be used to visualize the -Gal epitope on porcine tissues.

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 the hyper-branched core tetrasaccharide motif of chloroviruses

Chemical synthesis of complex oligosaccharides, especially those possessing hyper-branched structures with one or multiple 1,2-cisglycosidic bonds, is a challenging task. Complementary reactivity of glycosyl donors and acceptors and proper tuning of the s

Carbon tetrachloride-free allylic halogenation-mediated glycosylations of allyl glycosides

The allylic bromination of allyl glycosides is conducted using NBS/AIBN reagents in (EtO)2CO and PhCF3 solutions, without using CCl4 as a solvent. The activated mixed halo-allyl glycosides led to glycosylations, mediated by a triflate, in a latent-active

Synthesis, Conformational Analysis, and Complexation Study of an Iminosugar-Aza-Crown, a Sweet Chiral Cyclam Analog

A new family of chiral C2 symmetric tetraazamacrocycles, coined ISAC for IminoSugar Aza-Crown, incorporating two iminosugars adopting a 4C1 conformation is disclosed. Multinuclear NMR experiments on the corresponding Cdsu

A Synthetic Carbohydrate-Protein Conjugate Vaccine Candidate against Klebsiella pneumoniae Serotype K2

Klebsiella pneumoniae causes pneumonia and liver abscesses in humans worldwide and contains virulence factor capsular polysaccharides and lipopolysaccharides linked to the cell wall. Although capsular polysaccharides are good antigens for vaccine producti

Preparation method of fondaparinux sodium disaccharide intermediate

The invention discloses a preparation method of fondaparinux sodium disaccharide intermediate. 1-O-substituent sulfonyl-2,3-bis-O-benzyl-4,6-O-benzylidene-beta-D-glucopyranose directly reacts with 1,6-dehydrated-2-deoxy-2-azido-3-O-acetyl-beta-D-glucopyranose to prepare the fondaparinux sodium disaccharide intermediate as shown in a formula I; and meanwhile, the fondaparinux sodium intermediate asshown in the formula I can be used as a raw material to synthesize fondaparinux sodium intermediate as shown in a formula IV. The preparation method is simple and small in steps, the yield is high, the atomic utilization rate is high, the three wastes are small, and the preparation method is suitable for industrial large-scale production. Please see the description for the formula.

Glycosyl Aldehydes: New Scaffolds for the Synthesis of Neoglycoconjugates via Bioorthogonal Oxime Bond Formation

The straightforward preparation of glycosyl neoconjugates by oxime (or hydrazone) bond formation represents a key bioorthogonal tool in chemical biology. However, when this strategy is employed by reacting the reducing end of the glycan moiety, the configuration and the stereochemical information is lost due to partial (or complete) opening of the glycan cyclic hemiacetal and the formation of the corresponding opened tautomers. We have completed the synthesis of a library of glycosyl aldehydes to be used as scaffold for the synthesis of neoglycoconjugates via oxime bond formation. These glycosyl aldehydes constitute a simple and accessible alternative to avoid loss of chiral information when conjugating, by oxime (or hydrazone) bonds, the aldehyde functionality present at the reducing end of natural carbohydrates.

Synthesis, kinetics and inhibition of Escherichia coli Heptosyltransferase I by monosaccharide analogues of Lipid A

Gram-negative bacteria comprise the majority of microbes that cause infections that are resistant to pre-existing antibiotics. The complex cell wall architecture contributes to their ability to form biofilms, which are often implicated in hospital-acquired infections. Biofilms promote antibiotic resistance by enabling the bacteria to survive hostile environments such as UV radiation, pH shifts, and antibiotics. The outer membrane of Gram-negative bacteria contains lipopolysaccharide (LPS), which plays a role in adhesion to surfaces and formation of biofilms. The main focus of this work was the synthesis of a library of glycolipids designed to be simplified analogues of the Lipid A, the membrane embedded portion component of LPS, to be tested as substrates or inhibitors of Heptosyltransferase I (HepI or WaaC, a glycosyltransferase enzyme involved in the biosynthesis of LPS). Fourteen analogues were synthesized successfully and characterized. While these compounds were designed to function as nucleophilic substrates of HepI, they all demonstrated mild inhibition of HepI. Kinetic characterization of inhibition mechanism identified that the compounds exhibited uncompetitive and mixed inhibition of HepI. Since both uncompetitive and mixed inhibition result in the formation of an Enzyme-Substrate-inhibitor complex, molecular docking studies (using AutoDock Vina) were performed, to identify potential allosteric binding site for these compounds. The inhibitors were shown to bind to a pocket formed after undergoing a conformational change from an open to a closed active site state. Inhibition of HepI via an allosteric site suggest that disruption of protein dynamics might be a viable mechanism for the inhibition of HepI and potentially other enzymes of the GT-B structural class.