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1,3,4,6-tetra-O-acetyl-2-N-azidoacetyl-2-deoxy-β-D-glucopyranose is a complex chemical compound derived from glucose. It features four acetyl groups and an azidoacetyl group attached to the 2-position of the glucose molecule, along with a deoxy group at the same position. 1,3,4,6-tetra-O-acetyl-2-N-azidoacetyl-2-deoxy-β-D-glucopyranose is integral in carbohydrate chemistry, particularly for the synthesis of glycoconjugates and glycosylated molecules. Its distinctive structure and functional groups render it valuable for a range of biological and chemical applications, such as a substrate for enzymes and a precursor in the preparation of glycoproteins and glycolipids. It is instrumental in carbohydrate biochemistry research and the development of novel drugs and materials.

1404472-50-9

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1404472-50-9 Usage

Uses

Used in Carbohydrate Chemistry:
1,3,4,6-tetra-O-acetyl-2-N-azidoacetyl-2-deoxy-β-D-glucopyranose is used as a key intermediate for the synthesis of glycoconjugates and glycosylated molecules, which are essential in various biological processes and have potential applications in drug development.
Used in Pharmaceutical Research:
In the pharmaceutical industry, 1,3,4,6-tetra-O-acetyl-2-N-azidoacetyl-2-deoxy-β-D-glucopyranose serves as a precursor for the preparation of glycoproteins and glycolipids, which are vital for understanding their roles in disease mechanisms and for the creation of new therapeutic agents.
Used in Enzyme Substrates:
1,3,4,6-tetra-O-acetyl-2-N-azidoacetyl-2-deoxy-β-D-glucopyranose is utilized as a substrate for enzymes involved in carbohydrate metabolism and modification, aiding in the study of enzymatic activity and the development of enzyme inhibitors or activators.
Used in Material Science:
In material science, 1,3,4,6-tetra-O-acetyl-2-N-azidoacetyl-2-deoxy-β-D-glucopyranose is employed in the development of new materials with specific properties, such as improved biocompatibility or targeted drug delivery systems, by leveraging its unique chemical structure and functional groups.

Check Digit Verification of cas no

The CAS Registry Mumber 1404472-50-9 includes 10 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 7 digits, 1,4,0,4,4,7 and 2 respectively; the second part has 2 digits, 5 and 0 respectively.
Calculate Digit Verification of CAS Registry Number 1404472-50:
(9*1)+(8*4)+(7*0)+(6*4)+(5*4)+(4*7)+(3*2)+(2*5)+(1*0)=129
129 % 10 = 9
So 1404472-50-9 is a valid CAS Registry Number.

1404472-50-9Downstream Products

1404472-50-9Relevant academic research and scientific papers

Direct One-Step Fluorescent Labeling of O-GlcNAc-Modified Proteins in Live Cells Using Metabolic Intermediates

Tan, Hong Yee,Eskandari, Razieh,Shen, David,Zhu, Yanping,Liu, Ta-Wei,Willems, Lianne I.,Alteen, Matthew G.,Madden, Zarina,Vocadlo, David J.

, p. 15300 - 15308 (2018)

The modification of proteins with O-linked N-acetylglucosamine (O-GlcNAc) by the enzyme O-GlcNAc transferase (OGT) has emerged as an important regulator of cellular physiology. Metabolic labeling strategies to monitor O-GlcNAcylation in cells have proven of great value for uncovering the molecular roles of O-GlcNAc. These strategies rely on two-step labeling procedures, which limits the scope of experiments that can be performed. Here, we report on the creation of fluorescent uridine 5′-diphospho-N-acetylglucosamine (UDP-GlcNAc) analogues in which the N-acyl group of glucosamine is modified with a suitable linker and fluorophore. Using human OGT, we show these donor sugar substrates permit direct monitoring of OGT activity on protein substrates in vitro. We show that feeding cells with a corresponding fluorescent metabolic precursor for the last step of the hexosamine biosynthetic pathway (HBP) leads to its metabolic assimilation and labeling of O-GlcNAcylated proteins within live cells. This one-step metabolic feeding strategy permits labeling of O-GlcNAcylated proteins with a fluorescent glucosamine-nitrobenzoxadiazole (GlcN-NBD) conjugate that accumulates in a time- and dose-dependent manner. Because no genetic engineering of cells is required, we anticipate this strategy should be generally amenable to studying the roles of O-GlcNAc in cellular physiology as well as to gain an improved understanding of the regulation of OGT within cells. The further expansion of this one-step in-cell labeling strategy should enable performing a range of experiments including two-color pulse chase experiments and monitoring OGT activity on specific protein substrates in live cells.

Glucosamine- and galactosamine- based monosaccharides with highly fluorinated motifs

Tomaszewska, Joanna,Kowalska, Karolina,Koroniak-Szejn, Katarzyna

, p. 1 - 13 (2016)

Synthesis of modified monosaccharides, derivatives of glucose and galactose, having a highly fluorinated chain, as a library of synthetic building blocks for hyaluronic acid (HA) modified subunits has been developed. “Click” chemistry has been employed as a strategy for the synthesis of these molecules. 1,2,3-triazole ring derivatives were obtained with good to excellent yields.

Selective Engineering of Linkage-Specific α2,6-N-Linked Sialoproteins Using Sydnone-Modified Sialic Acid Bioorthogonal Reporters

Chinoy, Zoeisha S.,Bodineau, Clément,Favre, Camille,Moremen, Kelley W.,Durán, Raúl V.,Friscourt, Frédéric

, p. 4281 - 4285 (2019)

The metabolic oligosaccharide engineering (MOE) strategy using unnatural sialic acids has recently enabled the visualization of the sialome in living systems. However, MOE only reports on global sialylation and dissected information regarding subsets of s

A chemoenzymatic approach toward the preparation of site-specific antibody-drug conjugates

Cai, Xiaoqing,Janda, Kim D.

, p. 3172 - 3175 (2015)

An efficient chemical synthesis of UDP-N-azidoacetylgalactosamine (UDP-GalNAz) is presented, while the value of this molecule was demonstrated through its attachment to an antibody Fc domain. Thus, the antibody was first degalactosylated, which was followed by loading of the UDP-GalNAz with a recombinant galactosyltransferase. This engineered Azide-Fc-N-glycan antibody was subsequently 'clicked' by a strain-promoted alkyne-azide cycloaddition reaction for site-specific attachment of a fluorescent probe. The principles detailed will allow for the facile preparation of chemically defined homogeneous antibody-drug conjugates (ADCs).

Synthesis of a novel fluorescent ruthenium complex with an appended Ac4GlcNAc moiety by click reaction

Cheng, Qi,Cui, Yalu,Xiao, Nao,Lu, Jishun,Fang, Chen-Jie

, p. 1 - 10 (2018)

The O-linked β-N-acetylglucosamine (O-GlcNAc) modification is an abundant post-translational modification in eukaryotic cells, which plays a fundamental role in the activity of many cells and is associated with pathologies like type II diabetes, Alzheimer’s disease or some cancers. However, the precise connexion between O-GlcNAc-modified proteins and their function in cells is largely undefined for most cases. Confocal microscopy is a powerful and effective tool for in-cell elucidation of the function of biological molecules. Chemical labeling of non-ultraviolet or non-fluorescent carbohydrates with fluorescent tag is an essential step that makes intra-cellular microscopic inspection possible. Here we report a strategy based on the 1,3-dipolar cycloaddition, called click chemistry, between unnatural N-acetylglucosamine (GlcNAc) analogues Ac4GlcNAc (substituted with an azido group) and the corresponding fluorescent tag Ru(bpy)2(Phen-alkyne)Cl2 (4) to synthesize the fluorescent dye Ru(bpy)2(Phen-Ac4GlcNAc)Cl2 (5) under mild and neutral reaction conditions. Moreover, 5 showed good stability, desirable fluorescence characteristics, and exhibited rather low levels of cytotoxicity against sensitive MCF-7 cells. Additionally, we have achieved successful fluorescent imaging of 5 transported in living MCF-7 cells. Cell images displayed that proteins are potentially labelled with 5 in the cytoplasm.

Peptoids and polyamines going sweet: Modular synthesis of glycosylated peptoids and polyamines using click chemistry

Fuerniss, Daniel,Mack, Timo,Hahn, Frank,Vollrath, Sidonie B. L.,Koroniak, Katarzyna,Schepers, Ute,Braese, Stefan

, p. 56 - 63 (2013)

Sugar moieties are present in a wide range of bioactive molecules. Thus, having versatile and fast methods for the decoration of biomimetic molecules with sugars is of fundamental importance. The glycosylation of peptoids and polyamines as examples of such biomimetic molecules is reported here. The method uses Cu-catalyzed azide alkyne cycloaddition to promote the reaction of azidosugars with either polyamines or peptoids. In addition, functionalized nucleic acids were attached to polyamines via the same route. Based on a modular solid-phase synthesis of peralkynylated peptoids with up to six alkyne groups, the latter were modified with azidosugar building blocks by using copper-catalyzed azide alkyne cycloadditions. In addition, the up-scaling of some particular azide-modified sugars is described.

Novel Liposomal Azido Mannosamine Lipids on Metabolic Cell Labeling and Imaging via Cu-Free Click Chemistry

Shen, Li,Cai, Kaimin,Yu, Jin,Cheng, Jianjun

, p. 2317 - 2322 (2019)

In comparison with the popular Ac4ManNAz applied as cell labels via Cu-free click chemistry, two novel azido mannosamine lipids with C6 and C12 esters on anomeric hydroxyl groups were prepared and encapsulated in a liposome delivery system, which enhanced chemical stabilities and showed good cell-metabolizable labeling efficiency on MDA-MB-231 cells with strong fluorescence after the treatment of DBCO-Cy5 by triazole formation via click chemistry.

Targeted Ultrasound-Assisted Cancer-Selective Chemical Labeling and Subsequent Cancer Imaging using Click Chemistry

Wang, Hua,Gauthier, Marianne,Kelly, Jamie R.,Miller, Rita J.,Xu, Ming,O'Brien, William D.,Cheng, Jianjun

, p. 5452 - 5456 (2016)

Metabolic sugar labeling followed by the use of reagent-free click chemistry is an established technique for in vitro cell targeting. However, selective metabolic labeling of the target tissues in vivo remains a challenge to overcome, which has prohibited the use of this technique for targeted in vivo applications. Herein, we report the use of targeted ultrasound pulses to induce the release of tetraacetyl N-azidoacetylmannosamine (Ac4ManAz) from microbubbles (MBs) and its metabolic expression in the cancer area. Ac4ManAz-loaded MBs showed great stability under physiological conditions, but rapidly collapsed in the presence of tumor-localized ultrasound pulses. The released Ac4ManAz from MBs was able to label 4T1 tumor cells with azido groups and significantly improved the tumor accumulation of dibenzocyclooctyne (DBCO)-Cy5 by subsequent click chemistry. We demonstrated for the first time that Ac4ManAz-loaded MBs coupled with the use of targeted ultrasound could be a simple but powerful tool for in vivo cancer-selective labeling and targeted cancer therapies.

Nanobody-Engineered Natural Killer Cell Conjugates for Solid Tumor Adoptive Immunotherapy

Chen, Ying,Cui, Kaisa,Gong, Liang,Hong, Haofei,Huang, Zhaohui,Li, Dan,Li, Jiuming,Li, Yanchun,Wu, Zhimeng,Yin, Yuan

, (2021/11/16)

Cancer immunotherapy based on natural killer (NK) cells is demonstrated to be a promising strategy. However, NK cells are deficient in ligands that target specific tumors, resulting in limited antitumor efficacy. Here, a glycoengineering approach to imitate the chimeric antigen receptor strategy and decorate NK cells with nanobodies to promote NK-based immunotherapy in solid tumors is proposed. Nanobody 7D12, which specifically recognizes the human epidermal growth factor receptor (EGFR) that is overexpressed on many solid tumors, is coupled to the chemically synthesized DBCO-PEG4-GGG-NH2 by sortase A-mediated ligation to generate DBCO-7D12. The NK92MI cells bearing azide groups are then equipped with DBCO-7D12 via bioorthogonal click chemistry. The resultant 7D12-NK92MI cells exhibit high specificity and affinity for EGFR-overexpressing tumor cells in vitro and in vivo by the 7D12-EGFR interaction, causing increased cytokine secretion to more effectively kill EGFR-positive tumor cells, but not EGFR-negative cancer cells. Importantly, the 7D12-NK92MI cells also show a wide anticancer spectrum and extensive tumor penetration. Furthermore, mouse experiments reveal that 7D12-NK92MI treatment achieves excellent therapeutic efficacy and outstanding safety. The authors’ works provide a cell modification strategy using specific protein ligands without genetic manipulation and present a potential novel method for cancer-targeted immunotherapy by NK cells.

The Bioorthogonal Isonitrile-Chlorooxime Ligation

Li, Mao,Monaco, Mattia R.,Rivera-Fuentes, Pablo,Sch?fer, Rebecca J. B.,Tirla, Alina,Wennemers, Helma

supporting information, p. 18644 - 18648 (2019/11/28)

Bioorthogonal reactions are valuable tools for the selective labeling and imaging of natural products and proteins. Here, we present the reaction between isonitriles and chlorooximes as a ligation that proceeds quickly (k ≈ 1 M-1 s-1

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