20838-44-2

Usage

Uses

Used in Biochemical Research:
3-NITROPHENYL-BETA-D-GLUCOPYRANOSIDE is used as a substrate for studying glycosidase enzymes, which are crucial in the hydrolysis of glycosidic bonds in various biological processes. Its application aids in understanding the mechanisms of enzyme-catalyzed hydrolysis and the development of potential therapeutic agents targeting these enzymes.
Used in Pharmaceutical Research:
In the pharmaceutical industry, 3-NITROPHENYL-BETA-D-GLUCOPYRANOSIDE serves as a chromogenic substrate for the detection and measurement of enzyme activity in biological samples. Its ability to be hydrolyzed by beta-glucosidase, leading to the release of 3-nitrophenol, allows for the quantification of enzyme activity using spectrophotometric methods. This capability is vital for assessing the efficacy of potential drugs and their impact on enzyme function.
Used in Enzyme Activity Assays:
3-NITROPHENYL-BETA-D-GLUCOPYRANOSIDE is utilized as a tool in enzyme activity assays, providing a means to monitor and quantify the activity of glycosidase enzymes. The change in color upon hydrolysis offers a visual and measurable indicator of enzymatic activity, which is essential for research and diagnostic purposes.
Used in Drug Development:
3-NITROPHENYL-BETA-D-GLUCOPYRANOSIDE plays a significant role in the development of therapeutic agents that target glycosidase enzymes. By studying the interactions between 3-NITROPHENYL-BETA-D-GLUCOPYRANOSIDE and enzymes, researchers can gain insights into the design of drugs that modulate enzyme activity, potentially leading to treatments for various diseases associated with abnormal glycosidase function.

Upstream product

• 52571-64-9 Tetra-O-acetyl-m-nitrophenyl-α-D-galactopyranosid 
• 74808-10-9 2,3,4,6-tetra-O-acetyl-D-galactopyranosyl trichloroacetimidate 
• 25878-60-8 D-galactose pentaacetate 
• 604-68-2 α-D-glucopyranose peracetylate 
• 554-84-7 meta-nitrophenol 
• 6118-37-2 1-O-(3′-nitrophenyl)-2,3,4,6-tetra-O-acetyl-β-D-glucopyranoside 
• 572-09-8 2,3,4,6-tetra-O-acetyl-α-D-glucopyranosyl bromide 

Relevant academic research and scientific papers

Strong Inhibition of Cholera Toxin B Subunit by Affordable, Polymer-Based Multivalent Inhibitors

Cholera is a potentially fatal bacterial infection that affects a large number of people in developing countries. It is caused by the cholera toxin (CT), an AB5 toxin secreted by Vibrio cholera. The toxin comprises a toxic A-subunit and a pentameric B-subunit that bind to the intestinal cell surface. Several monovalent and multivalent inhibitors of the toxin have been synthesized but are too complicated and expensive for practical use in developing countries. Meta-nitrophenyl α-galactoside (MNPG) is a known promising ligand for CT, and here mono- and multivalent compounds based on MNPG were synthesized. We present the synthesis of MNPG in greatly improved yields and its use while linked to a multivalent scaffold. We used economical polymers as multivalent scaffolds, namely, polyacrylamide, dextran, and hyperbranched polyglycerols (hPGs). Copper-catalyzed alkyne azide cycloaddition reaction (CuAAC) produced the inhibitors that were tested in an ELISA-type assay and an intestinal organoid swelling inhibition assay. The inhibitory properties varied widely depending on the type of polymer, and the most potent conjugates showed IC50 values in the nanomolar range.

PHENOL GLYCOSIDES AND THEIR USE IN THE TREATMENT OF UROLITHIASIS

The present invention relates to novel derivatives of polyphenol glycoside or polyalcohols of formula (1), wherein R1, R2, R3 is selected from the group consisting of H, OH, C(O)R4, C(0) OR4, 0 (Gly H3)n, wherein n = 0 1, 2, 3, and R4 is selected from the group consisting of H, alkyl, and Gly is a mono- or disaccharide residue. The present invention also relates to novel derivatives of glycoside polyphenols or polyalcohols, as pharmaceutical composition comprising a novel polyphenol glycoside or polyalcohols and the use of novel polyphenol glycoside or polyalcohols for the treatment of urolithiasis.

Solid-phase oligosaccharide and glycopeptide synthesis using glycosynthases

Enzymatic approaches for the preparation of oligosaccharides are interesting alternatives to traditional chemical synthesis, the main advantage being the regio- and stereoselectivity offered without the need for protecting groups. The use of solid-phase techniques offers easy workup procedures and the prospect of automatability. Here, we report the first application of glycosynthases to solid-phase oligosaccharide synthesis by use of the 51 kDa serine and glycine mutants of Agrobacterium sp. β-glucosidase, Abg E358S and E358G. Acceptors were linked to PEGA resin through a backbone amide linker (BAL), and using these mutated enzymes, a galactose moiety was transferred from a donor sugar, α-D-galactosyl fluoride, with high efficiency (>90%) together with excellent recovery of material. Furthermore, it was demonstrated that a resin-bound model glycopeptide was also an acceptor for the glycosynthase.