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1,3,4,6-tetra-O-acetyl-2-deoxy-2-(2,2,2-trichloroethoxycarbonylamino)-β-D-glucopyranose is a complex chemical compound derived from glucose. It features acetyl and trichloroethoxycarbonylamino groups attached to the sugar molecule, providing unique properties for its applications in various fields.

122210-05-3

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122210-05-3 Usage

Uses

Used in Organic Chemistry:
1,3,4,6-tetra-O-acetyl-2-deoxy-2-(2,2,2-trichloroethoxycarbonylamino)-β-D-glucopyranose is used as a protective group for the hydroxyl groups of glucose. This allows for selective modification of the molecule, facilitating the synthesis of various carbohydrate derivatives and glycoconjugates.
Used in Pharmaceutical Research:
In the pharmaceutical industry, 1,3,4,6-tetra-O-acetyl-2-deoxy-2-(2,2,2-trichloroethoxycarbonylamino)-β-D-glucopyranose is utilized in the synthesis of carbohydrate-based drugs and therapeutic agents. Its unique structure and protective group properties enable the development of novel compounds with potential medicinal applications.
Used in Carbohydrate Chemistry:
1,3,4,6-tetra-O-acetyl-2-deoxy-2-(2,2,2-trichloroethoxycarbonylamino)-β-D-glucopyranose is employed as a key intermediate in carbohydrate chemistry. The trichloroethoxycarbonylamino group serves as a common protecting group, allowing for the manipulation of specific hydroxyl groups while preserving the overall structure of the sugar molecule. This enables researchers to explore the synthesis of diverse carbohydrate derivatives with tailored properties for various applications.

Check Digit Verification of cas no

The CAS Registry Mumber 122210-05-3 includes 9 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 6 digits, 1,2,2,2,1 and 0 respectively; the second part has 2 digits, 0 and 5 respectively.
Calculate Digit Verification of CAS Registry Number 122210-05:
(8*1)+(7*2)+(6*2)+(5*2)+(4*1)+(3*0)+(2*0)+(1*5)=53
53 % 10 = 3
So 122210-05-3 is a valid CAS Registry Number.

122210-05-3Relevant academic research and scientific papers

O-GlcNAcylation of truncated NAC segment alters peptide-dependent effects on α-synuclein aggregation

Davey, Andrew K.,Kassiou, Michael,Mellick, George D.,Rudrawar, Santosh,Ryan, Philip,Xu, Ming-ming

, (2019)

Numerous post-translational modifications (PTMs) of the Parkinson's disease (PD) associated α-synuclein (α-syn) protein have been recognised to play critical roles in disease aetiology. Indeed, dysregulated phosphorylation and proteolysis are thought to modulate α-syn aggregation and disease progression. Among the PTMs, enzymatic glycosylation with N-acetylglucosamine (GlcNAc) onto the protein's hydroxylated amino acid residues is reported to deliver protective effects against its pathogenic processing. This modification has been reported to alter its pathogenic self-assembly. As such, manipulation of the protein's O-GlcNAcylation status has been proposed to offer a PD therapeutic route. However, targeting upstream cellular processes can lead to mechanism-based toxicity as the enzymes governing O-GlcNAc cycling modify thousands of acceptor substrates. Small glycopeptides that couple the protective effects of O-GlcNAc with the selectivity of recognition sequences may prove useful tools to modulate protein aggregation. Here we discuss efforts to probe the effects of various O-GlcNAc modified peptides on wild-type α-synuclein aggregation.

Rational Design of a DNA-Scaffolded High-Affinity Binder for Langerin

Bachem, Gunnar,Baukmann, Hannes,Dernedde, Jens,Fuchsberger, Felix,Kim, Dongyoon,Rademacher, Christoph,Seitz, Oliver,Silberreis, Kim,Wamhoff, Eike-Christian

, p. 21016 - 21022 (2020)

Binders of langerin could target vaccines to Langerhans cells for improved therapeutic effect. Since langerin has low affinity for monovalent glycan ligands, highly multivalent presentation has previously been key for targeting. Aiming to reduce the amoun

Regioselective phenol or carbinol glycosidation of 17β-estradiol and derivatives thereof

Adinolfi, Matteo,Iadonisi, Alfonso,Pezzella, Alessandro,Ravidà, Alessandra

, p. 1848 - 1852 (2005)

Unprecedented regioselective glycosidations of 17β-estradiol and nitro substituted derivatives thereof either at the phenol or carbinol position is reported. In the former case, glycosyl bromides or iodides were employed as the donors in a base promoted reaction conducted under two-phase conditions. In the latter case, glycosyl trichloroacetimidate donors were used in combination with the mild activation of 4 A? acid washed molecular sieves. Georg Thieme Verlag Stuttgart.

Dual-tail approach to discovery of novel carbonic anhydrase IX inhibitors by simultaneously matching the hydrophobic and hydrophilic halves of the active site

Hou, Zhuang,Lin, Bin,Bao, Yu,Yan, Hai-ning,Zhang, Miao,Chang, Xiao-wei,Zhang, Xin-xin,Wang, Zi-jie,Wei, Gao-fei,Cheng, Mao-sheng,Liu, Yang,Guo, Chun

, p. 1 - 10 (2017)

Dual-tail approach was employed to design novel Carbonic Anhydrase (CA) IX inhibitors by simultaneously matching the hydrophobic and hydrophilic halves of the active site, which also contains a zinc ion as part of the catalytic center. The classic sulfanilamide moiety was used as the zinc binding group. An amino glucosamine fragment was chosen as the hydrophilic part and a cinnamamide fragment as the hydrophobic part in order to draw favorable interactions with the corresponding halves of the active site. In comparison with sulfanilamide which is largely devoid of the hydrophilic and hydrophobic interactions with the two halves of the active site, the compounds so designed and synthesized in this study showed 1000-fold improvement in binding affinity. Most of the compounds inhibited the CA effectively with IC50 values in the range of 7–152?nM. Compound 14e (IC50: 7?nM) was more effective than the reference drug acetazolamide (IC50: 30?nM). The results proved that the dual-tail approach to simultaneously matching the hydrophobic and hydrophilic halves of the active site by linking hydrophobic and hydrophilic fragments was useful for designing novel CA inhibitors. The effectiveness of those compounds was elucidated by both the experimental data and molecular docking simulations. This work laid a solid foundation for further development of novel CA IX inhibitors for cancer treatment.

A facile and efficient method for synthesis of macrocyclic lipoglycopeptide

Zhao, Qingjie,Li, Xiang,Li, Wenjuan,Zou, Yan,Hu, Honggang,Wu, Qiuye

, p. 1018 - 1022 (2015)

An efficient and practical method for macrocyclic lipoglycopeptide synthesis was developed and utilized to synthesize lipoglycosylated derivatives of Tyrocidine A. The method is based on solid-phase peptide synthesis using 2-chlorotrityl resin as the soli

Glycosylation with N-Troc-protected glycosyl donors

Ellervik, Ulf,Magnusson, Goeran

, p. 251 - 260 (1996)

N-Troc-protected (Troc = 2,2,2-trichloroethoxycarbonyl) glucosamine and galactosamine glycosyl donors (1-O-acetyl sugar, bromo sugar, and thioglycoside) were compared with the corresponding N-Phth-protected derivatives in glycosylations of 2-(trimethylsilyl)ethanol, 2-bromoethanol, methyl 3-mercaptopropionate, N-Fmoc-protected serine, and 2-(trimethylsilyl)ethyl 6-O-benzyl-2-deoxy-2-phthalimido-β-D-glucopyranoside. The N-Troc-protected donors gave pure β-glycosides in somewhat higher yields than the N-Phth-protected counterparts. The N-Troc protecting group can be removed by reduction with zinc, which allows selective N-deprotection in oligosaccharides containing both N-Troc and N-Phth groups.

Synthesis of ureido thioglycosides as novel insect β?N?acetylhexosaminidase OfHex1 inhibitors

Dong, Lili,Dong, Yanhong,Lu, Huizhe,Shen, Shengqiang,Yang, Qing,Zhang, Jianjun

, (2020)

The insect β-N-acetylhexosaminidase OfHex1 from Ostrinia furnacalis (one of the most destructive agricultural pests) has been considered as a promising pesticide target. In this study, a series of novel and readily available ureido thioglycosides were designed and synthesized based on the catalytic mechanism and the co-crystal structures of OfHex1 with substrates. After evaluation via enzyme inhibition experiments, thioglycosides 11c and 15k were found to have inhibitory activities against OfHex1 with the Ki values of 25.6 μM and 53.8 μM, respectively. In addition, all these ureido thioglycosides exhibited high selectivity toward OfHex1 over hOGA and HsHexB (Ki > 100 μM). Furthermore, to investigate the inhibitory mechanism, the possible binding modes of 11c and 15k with OfHex1 were deduced based on molecular docking analysis. This work may provide useful structural starting points for further rational design of potent inhibitors of OfHex1.

Synthesis and cytotoxicity of the conjugates of diterpenoid isosteviol and N-acetyl-D-glucosamine

Garifullin, Bulat F.,Strobykina, Irina Yu.,Khabibulina, Leysan R.,Sapunova, Anastasiya S.,Voloshina, Aleksandra D.,Sharipova, Radmila R.,Khairutdinov, Bulat I.,Zuev, Yuriy F.,Kataev, Vladimir E.

, p. 1372 - 1378 (2019/08/22)

A series of conjugates of diterpenoid isosteviol (16-oxo-ent-beyeran-19-oic acid) and N-acetyl-D-glucosamine was synthesised and their cytotoxicity against several human cancer cell lines (M-Hela, MCF-7, Hep G2, Panc-1, PC-3), as well as normal human cell lines (WI-38, Chang liver) was assayed. Most of the conjugates were found to be cytotoxic against the mentioned cancer cell lines in the range of IC50 values 13–89 μM. Two lead compounds 14a and 14b showed selective cytotoxicity against M-Hela (IC50 13 and 14 μM) that was two times as high as the cytotoxicity of the anti-cancer drug Tamoxifen in control (IC50 28 μM). It was found that cytotoxic activity of the lead compounds against M-Hela cells is due to induction of apoptosis.

Novel carbohydrate-based sulfonamide derivatives as selective carbonic anhydrase II inhibitors: Synthesis, biological and molecular docking analysis

Hou, Zhuang,Cai, Qiang,Cheng, Mao-sheng

supporting information, (2021/09/28)

A series of sulfonamides containing glucosamine moieties had been prepared and investigated for the inhibition of the zinc enzyme carbonic anhydrases (CAs, EC 4.2.1.1). Compared to their parent compound p-sulfamoylbenzoic acid, target compounds showed two order of magnitude improvement in their binding affinities against hCA II in vitro. Moreover, they also showed great selectivity toward hCA II enzyme with the ratios for inhibiting hCA II over hCA I in the range 20–96 and for inhibiting hCA II over hCA IX in the range 4.3–9. Due to the introduction of glucosamine moieties, all of compounds displayed good water solubility (in the range of 2.0–2.5%) and the pH values of the obtained solutions is neutral (7.0–7.2). Compared to the clinically available and relatively highly acidic dorzolamide (pH 5.5), target compounds are more likely to be less irritating to the eye when applied to topical glaucomatous drugs. Then, cytotoxicity evaluation suggested that all target compounds did not display any appreciable toxicity against human cornea epithelial cell. In addition, molecular docking studies elucidated the binding modes of those compounds toward hCA II. Collectively, these results suggest that target compounds represented a promising scaffold to treat glaucoma without major topical side effects.

Self-Promoted Glycosylation for the Synthesis of β-N-Glycosyl Sulfonyl Amides

Ma?a, Patrycja,Pedersen, Christian Marcus

supporting information, p. 5685 - 5689 (2021/08/30)

N-Glycosyl N-sulfonyl amides have been synthesized by a self-promoted glycosylation, i. e. without any catalysts, promotors or additives. When the reactions were carried out at lower temperatures a mixture of N- and O-glycosides were observed, where the latter rearranged to give the β-N-glycosides at elevated temperatures. By this method sulfonylated asparagine derivatives can be selectively β-glycosylated in high yields by trichloroacetimidate glycosyl donors of different reactivity including protected glucosamine derivatives. The chemoselectivity in the glycosylations as well as the rearrangements from O-glycosides to β-N-glycosides gives information of the glycosylation mechanism. This method gives access to glycosyl sulfonyl amides under mild conditions.

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