10378-06-0Relevant articles and documents
Water-soluble Glucosamine-coated AIE-Active Fluorescent Organic Nanoparticles: Design, Synthesis and Assembly for Specific Detection of Heparin Based on Carbohydrate–Carbohydrate Interactions
Ji, Yan-ming,Liu, Guang-jian,Li, Cui-yun,Liu, Yi-chen,Hou, Min,Xing, Guo-wen
, p. 3295 - 3300 (2019)
Two water-soluble carbohydrate-coated AIE-activate fluorescent organic nanoparticles TPE3G and TPE4G were designed and synthesized for the detection of heparin. Different from the reported strategy, we not only utilized the general detection mechanism of
CONVENIENT METHOD FOR SYNTHESIS OF 2-METHYL-GLYCO-2-OXAZOLINES
Bovin, N. V.,Zurabyan, S. E.,Khorlin, A. Ya.
, p. 2339 - 2340 (1981)
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A facile and quantitative preparation of activated cyclic sugar derivatives using HgBr2 and 2,4,6-collidine
Matsuoka,Nishimura,Lee
, p. 1715 - 1720 (1995)
A combination of mercury(II) bromide (HgBr2) and 2,4,6-collidine was found to promote the formation of activated cyclic sugar derivatives such as 1,2-orthoesters and an oxazoline derivative in quantitative yields at room temperature. A slightly hindered skew like conformation of the lactose orthoester derivative was revealed by 1H NMR analysis. It was also suggested that the reaction of a lactose 1,2-orthoester with trimethylsilyl azide proceeded smoothly to give β-lactosyl azide stereoselectively which is a useful intermediate for constructing glycopeptides and neoglycoconjugates.
Effect of fluorous tags on glycosylation of saccharide primers in animal cells
Kasuya, Maria Carmelita Z.,Tojino, Mami,Nakano, Shinya,Mizuno, Mamoru,Hatanaka, Kenichi
, p. 1409 - 1415 (2009)
A series of fluorous-tagged saccharide primers with different contents of fluorous atoms was synthesized and introduced into mouse melanoma B16 cells. The primers did not affect cell morphology and viability at a concentration of 50 μM. The numerous fluorine atoms did not pose a steric barrier to primer assimilation into cells and did not affect cellular-enzyme-catalyzed glycosylation. The lactoside primers were sialylated to afford GM3-type oligosaccharide. On the other hand, the GlcNAc primers were galactosylated to afford a lactosamine derivative that was further sialylated by cellular enzymes to afford a sialylated lactosamine.
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Nashed et al.
, p. C13 (1977)
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Design, Synthesis, and Preliminary Biological Evaluation of GlcNAc-6P Analogues for the Modulation of Phosphoacetylglucosamine Mutase 1 (AGM1/PGM3)
Paiotta, Alice,D'Orazio, Giuseppe,Palorini, Roberta,Ricciardiello, Francesca,Zoia, Luca,Votta, Giuseppina,De Gioia, Luca,Chiaradonna, Ferdinando,La Ferla, Barbara
, p. 1946 - 1952 (2018)
A library of GlcNAc 6- or 1-phosphate analogues was designed, and each compound was evaluated computationally through docking studies for its binding affinity to AGM1/PGM3. The compounds with the highest binding affinity, as ranked through a docking score, were synthesised and screened for their ability to inhibit the production of UDP-GlcNAc. A glycofused oxazoline analogue showed good inhibition, and gave significant results in vitro.
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Chorlin et al.
, p. 2094,2097; engl. Ausg. S. 1987, 1989 (1968)
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Simple and Efficient Preparation of O- and S-GlcNAcylated Amino Acids through InBr3-Catalyzed Synthesis of β- N-Acetylglycosides from Commercially Available Reagents
De Leon, Cesar A.,Lang, Geoffrey,Saavedra, Marcos I.,Pratt, Matthew R.
, p. 5032 - 5035 (2018)
The facile synthesis of serine, threonine, and cysteine β-glycosides using commercially available peracetylated β-N-acetylglucosamine (β-Ac4GlcNAc) and catalytic amounts of indium bromide (InBr3) is described. This method involves only inexpensive reagents that require no further modification or special handling. The reagents are simply mixed, dissolved, and refluxed to afford the GlcNAcylated amino acids in great yields (70-80%). This operationally simple procedure should facilitate the study of O-GlcNAcylation without necessitating expertise in synthetic carbohydrate chemistry.
A new procedure for the preparation of oligosaccharide oxazolines.
Nakabayashi,Warren,Jeanloz
, p. C7 - C10,C7-10 (1986)
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Photo-click immobilization on quartz crystal microbalance sensors for selective carbohydrate-protein interaction analyses
Norberg, Oscar,Deng, Lingquan,Aastrup, Teodor,Yan, Mingdi,Ramstroem, Olof
, p. 1000 - 1007 (2011)
A photoclick method based on azide photoligation and Cu-catalyzed azide-alkyne cycloaddition has been evaluated for the immobilization of carbohydrates to polymeric materials. The biomolecular recognition properties of the materials have been investigated with regard to applicable polymeric substrates and selectivity of protein binding. The method was used to functionalize a range of polymeric surfaces (polystyrene, polyacrylamide, polyethylene glycol), poly(2-ethyl-2-oxazoline), and polypropene) with various carbohydrate structures (based on α-D-mannose, β-D-galactose, and N-acetyl-β-D-glucosamine). The functionalized surfaces were evaluated in real-time studies of protein-carbohydrate interactions using a quartz crystal microbalance flow-through system with a series of different carbohydrate-binding proteins (lectins). The method proved to be robust and versatile, resulting in a range of efficient sensors showing high and predictable protein selectivities.
De novo design of a trans-β-N-acetylglucosaminidase activity from a GH1 β-glycosidase by mechanism engineering
André-Miral, Corinne,Koné, Fankroma Mt,Solleux, Claude,Grandjean, Cyrille,Dion, Michel,Tran, Vinh,Tellier, Charles
, p. 394 - 402 (2015)
Glycoside hydrolases are particularly abundant in all areas of metabolism as they are involved in the degradation of natural polysaccharides and glycoconjugates. These enzymes are classified into 133 families (CAZy server, http://www.cazy.org) in which members of each family have a similar structure and catalytic mechanism. In order to understand better the structure/function relationships of these enzymes and their evolution and to develop new robust evolved glycosidases, we undertook to convert a Family 1 thermostable β-glycosidase into an exo-β-N-acetylglucosaminidase. This latter activity is totally absent in Family 1, while natural β-hexosaminidases belong to CAZy Families 3, 20 and 84. Using molecular modeling, we first showed that the docking of N-acetyl-d-glucosamine in the subsite -1 of the β-glycosidase from Thermus thermophilus (TtβGly) suggested several steric conflicts with active site amino-acids (N163, E338) induced by the N-acetyl group. Both N163A and N163D-E338G mutations induced significant N-acetylglucosaminidase activity in TtβGly. The double mutant N163D-E338G was also active on the bicyclic oxazoline substrate, suggesting that this mutated enzyme uses a catalytic mechanism involving a substrate-assisted catalysis with a noncovalent oxazoline intermediate, similar to the N-acetylglucosaminidases from Families 20 and 84. Furthermore, a very efficient trans-N-acetylglucosaminidase activity was observed when the double mutant was incubated in the presence of NAG-oxazoline as a donor and N-methyl-O-benzyl-N-(β-d-glucopyranosyl)-hydroxylamine as an acceptor. More generally, this work demonstrates that it is possible to exchange the specificities and catalytic mechanisms with minimal changes between phylogenetically distant protein structures.
A silyl ether-protected building block forO-GlcNAcylated peptide synthesis to enable one-pot acidic deprotection
Yan, Bingjia,Li, Wenyi,Hackenberger, Christian P. R.
supporting information, p. 8014 - 8017 (2021/10/04)
In this report, we introduce a novel building block for Fmoc/tBu solid phase peptide synthesis (SPPS) of β-linkedO-GlcNAcylated peptides. This building block carries acid labile silyl ether protecting groups, which are fully removed under TFA-mediated peptide cleavage conditions from the resin, thus requiring fewer synthetic steps and no intermediate purification as compared to other acid or base labile protecting group strategies.
Dual-participation protecting group solves the anomeric stereocontrol problems in glycosylation reactions
Liu, Hui,Hansen, Thomas,Zhou, Si-Yu,Wen, Guo-En,Liu, Xu-Xue,Zhang, Qing-Ju,Codeé, Jeroen D. C.,Schmidt, Richard R.,Sun, Jian-Song
supporting information, p. 8713 - 8717 (2019/10/28)
The 2,2-dimethyl-2-(ortho-nitrophenyl)acetyl (DMNPA) group permits, via robust neighboring group participation (NGP) or long distance participation (LDP) effects, the stereocontrolled 1,2-trans, 1,2-cis, as well as β-2,6-dideoxy glycosidic bond generation, while suppressing the undesired orthoester byproduct formation. The robust stereocontrol capability of the DMNPA is due to the dual-participation effect from both the ester functionality and the nitro group, verified by control reactions and DFT calculations and further corroborated by X-ray spectroscopy.