2872-66-4

Usage

Uses

Used in Organic Synthesis:
1-(4-NITROPHENYL)-2,3,4,6-TETRA-O-ACETYL-BETA-D-GALACTOPYRANOSIDE is used as a synthetic intermediate for the preparation of various organic compounds. Its unique structure allows for selective reactions and modifications, making it a valuable building block in the synthesis of complex organic molecules.
Used in Pharmaceutical Industry:
1-(4-NITROPHENYL)-2,3,4,6-TETRA-O-ACETYL-BETA-D-GALACTOPYRANOSIDE is used as a key component in the development of pharmaceutical compounds. Its ability to form stable derivatives and its reactivity make it suitable for the synthesis of drug candidates with potential therapeutic applications.
Used in Chemical Research:
1-(4-NITROPHENYL)-2,3,4,6-TETRA-O-ACETYL-BETA-D-GALACTOPYRANOSIDE is used as a research tool in chemical laboratories. Its unique properties and reactivity enable scientists to study various chemical reactions and mechanisms, contributing to the advancement of chemical knowledge and the development of new synthetic methods.
Used in Analytical Chemistry:
1-(4-NITROPHENYL)-2,3,4,6-TETRA-O-ACETYL-BETA-D-GALACTOPYRANOSIDE is used as a reference compound in analytical chemistry. Its distinct chemical properties and spectral characteristics make it suitable for calibration and validation of analytical instruments and methods, ensuring accurate and reliable measurements in various applications.

InChI:InChI=1/C20H23NO12/c1-10(22)28-9-16-17(29-11(2)23)18(30-12(3)24)19(31-13(4)25)20(33-16)32-15-7-5-14(6-8-15)21(26)27/h5-8,16-20H,9H2,1-4H3/t16-,17+,18+,19-,20-/m1/s1

Upstream product

• 100-02-7 4-nitro-phenol 
• 3068-32-4 1-bromo-1-deoxy-2,3,4,6-tetra-O-acetyl-a-D-galactopyranoside 
• 4163-60-4 β-D-galactose peracetate 
• 108-24-7 acetic anhydride 
• 3150-24-1 4-nitrophenyl-β-D-galactopyranoside 
• 3947-62-4 2,3,4,6-tetra-O-acetyl-α/β-D-galactopyranose 
• 1420786-80-6 C₂₉H₂₈O₁₁ 
• 824-78-2 4-nitrophenol sodium salt 
• 10257-28-0 D-Galactose 
• 25878-60-8 D-galactose pentaacetate 
• 7512-17-6 N-Acetyl-D-glucosamine 
• 86520-63-0 2,3,4,6-tetra-O-acetyl-α-galactopyranosyl trichloroacetimidate 
• 3068-32-4 1-bromo-2,3,4,6-tetra-O-acetyl-D-galactopyranose 
• 24067-17-2 4-nitrophenylboronic acid 

Downstream Products

• 3150-24-1 4-nitrophenyl-β-D-galactopyranoside 
• 170940-41-7 Acetic acid (2S,3R,4S,5S,6R)-4,5-diacetoxy-6-acetoxymethyl-2-(4-acetylamino-phenoxy)-tetrahydro-pyran-3-yl ester 
• 42011-36-9 (2R,3S,4S,5R,6S)-2-(acetoxymethyl)-6-(4-aminophenoxy)tetrahydro-2H-pyran-3,4,5-triyl triacetate 
• 4163-60-4 β-D-galactose peracetate 
• 17042-39-6 p-nitrophenyl 2,3,4,6-tetra-O-acetyl-α-D-galactopyranoside 
• 1427462-40-5 5-(-N-(p-O-(2,3,4,6-tetra-O-acetyl-β-D-galactosyl)phenyl)-aminocarbonyl)-2,2'-bipyridine 
• 1427462-44-9 5-(-N-(p-O-(β-D-galactosyl)phenyl)-aminocarbonyl)-2,2'-bipyridine 
• 5094-33-7 p-aminophenyl β-D-galactopyranoside 

Relevant academic research and scientific papers

Nitrogen-containing aromatic ring derivative containing galactose and application thereof

The invention belongs to the technical field of medicines, and relates to a nitrogen-containing aromatic ring derivative containing galactose, application thereof and a pharmaceutical composition containing the compound. The invention also relates to a method for preparing the compound and the pharmaceutical composition, and application of the compound and the pharmaceutical composition in prevention or treatment of tumors, inflammatory diseases, autoimmune diseases and other diseases, especially tumors.

Copper-mediated O-arylation of lactols with aryl boronic acids

An efficient and novel methodology to access phenolic glycosides has been established by using copper-mediated coupling reaction of aryl boronic acids with hemiacetals. The reaction takes place normally in the presence of Cu(OAc)2 (1.0 equiv.) and pyridine (2.0 equiv.) at 40 °C. This protocol distinguishes itself by wide substrate scope, operational simplicity and giving rise to a myriad of phenolic glycosides in good to excellent yields.

Chemo-enzymatic synthesis of p-nitrophenyl β-D-galactofuranosyl disaccharides from Aspergillus sp. fungal-type galactomannan

β-D-Galactofuranose (Galf) is a component of polysaccharides and glycoconjugates. There are few reports about the involvement of galactofuranosyltransferases and galactofuranosidases (Galf-ases) in the synthesis and degradation of galactofuranose-containing glycans. The cell walls of filamentous fungi in the genus Aspergillus include galactofuranose-containing polysaccharides and glycoconjugates, such as O-glycans, N-glycans, and fungal-type galactomannan, which are important for cell wall integrity. In this study, we investigated the synthesis of p-nitrophenyl β-D-galactofuranoside and its disaccharides by chemo-enzymatic methods including use of galactosidase. The key step was selective removal of the concomitant pyranoside by enzymatic hydrolysis to purify p-nitrophenyl β-D-galactofuranoside, a promising substrate for β-D-galactofuranosidase from Streptomyces species.

Development of Pseudomonas aeruginosa Lectin LecA Inhibitor by using Bivalent Galactosides Supported on Polyproline Peptide Scaffolds

LecA is a galactose-binding tetrameric lectin from Pseudomonas aeruginosa involved in infection and biofilm formation. The emergent antibiotic resistance of P. aeruginosa has made LecA a promising pharmaceutical target to treat such infections. To develop LecA inhibitors, we exploit the unique helical structure of polyproline peptides to create a scaffold that controls the galactoside positions to fit their binding sites on LecA. With a modular scaffold design, both the galactoside ligands and the inter-ligand distance can be altered conveniently. We prepared scaffolds with spacings of 9, 18, 27, and 36 ? for ligand conjugation and found that glycopeptides with galactosides ligands three helical turns (27 ?) apart best fit LecA. In addition, we tested different galactose derivatives on the selected scaffold (27 ?) to improve the binding avidity to LecA. The results validate a new multivalent scaffold design and provide useful information for LecA inhibitor development.

Beta-galactosidase-responsive synthetic biomarker for targeted tumor detection

Tumor biomarkers are highly desirable for the screening of patients with a risk of tumor development and progression. Here, we report a beta-galactosidase (β-gal)-responsive acetaminophen (β-GR-APAP) as a synthetic plasma biomarker for targeted tumor detection. Tumor β-gal labeling via the recognition of tumor-related antigen enabled the detection of a tumor using β-GR-APAP.

Diazepinium perchlorate: a neutral catalyst for mild, solvent-free acetylation of carbohydrates and other substances

Diazepinium perchlorate, an essentially neutral organic salt possessing excellent stability, has been found to be well suited for the acetylation of free as well as partially protected sugars, phenols, thiophenols, thiols and other alcohols as well as amines. The diazepinium perchlorate-catalyzed acetylation is mild, organic and solvent-free and leaves acid sensitive protecting groups such as TBDMS/TBDPS/Tr ethers and isopropylidene/benzylidene acetals present on a substrate unaffected. Regioselective hydroxyl protection in partially protected carbohydrate derivatives/polyhydroxylic compounds was possible and was proved to be a convenient time-saving alternative to the conventional synthesis of such compounds. Easy preparation of the catalyst, mild reaction conditions and an environmentally benign protocol are some of the notable features of this reaction. The results obtained on the acetylation of phenols and thiophenols could be rationalized through their local nucleophilicity index obtained from DFT calculations.

Synthetic multivalent ligands for cholera & cholera-like toxins: Protected cyclic neoglycopeptides

Synthesis of a set of novel glycopeptide analogues as potential cholera/cholera-like toxin inhibitors in their protected form is described. They include di-, tri-, tetra- and pentavalent scaffolds. The synthetic steps were achieved using a combination of solvent-free mechanochemical as well as the conventional solution-phase reactions. During the conventional DIC-HOBt-mediated peptide coupling followed for the preparation of certain glycopeptide analogues an interesting in situ Fmoc deprotection was observed which has been demonstrated to hold potential for synthesiszing glycopeptides/neoglycopeptides with extended polyamide chains.

Preparation method of galactose-containing fatty acid derivative and application of preparation method in field of medicine

The invention relates to a novel p-fatty alkylamide phenyl-beta-D-galactoside compound, a preparation method and application, belonging to the technical field of medicine. A structure general formula of the compound is shown in the description, wherein R is selected from (CH2)6CH3, (CH2)10CH3, (CH2)12CH3, (CH2)14CH3, and (CH2)7CH=CH (CH2)7CH3. The compound has stronger inhibitory activity to tumor cells, and can be used for tumor therapies.

Glycosylated lanthanide cyclen complexes as luminescent probes for monitoring glycosidase enzyme activity

The development of synthetic chemical probes for the detection of enzymes is extremely important for biological, medicinal, and industrial applications. Here we report the synthesis of an array of novel glycosylated Tb(iii) complexes, their photophysical properties in solution, and their ability to function as luminescent probes for observing glycosidase enzyme activity in real time. Our initial studies into the application of these complexes for the detection of the Concanavalin A (ConA) lectin is also reported, highlighting the broad scope of these novel chemical probes.

Development and optimization of a competitive binding assay for the galactophilic low affinity lectin LecA from: Pseudomonas aeruginosa

Infections with the Gram-negative bacterium Pseudomonas aeruginosa result in a high mortality among immunocompromised patients and those with cystic fibrosis. The pathogen can switch from planktonic life to biofilms, and thereby shields itself against antibiotic treatment and host immune defense to establish chronic infections. The bacterial protein LecA, a C-type lectin, is a virulence factor and an integral component for biofilm formation. Inhibition of LecA with its carbohydrate ligands results in reduced biofilm mass, a potential Achilles heel for treatment. Here, we report the development and optimization of a fluorescence polarization-based competitive binding assay with LecA for application in screening of potential inhibitors. As a consequence of the low affinity of d-galactose for LecA, the fluorescent ligand was optimized to reduce protein consumption in the assay. The assay was validated using a set of known inhibitors of LecA and IC50 values in good agreement with the known Kd values were obtained. Finally, we employed the optimized assay to screen sets of synthetic thio-galactosides and natural blood group antigens and report their structure-activity relationship. In addition, we evaluated a multivalent fluorescent assay probe for LecA and report its applicability in an inhibition assay.