Efficient Synthesis of Sugar Oxazolines from Unprotected <i>N</i>-Acetyl-2-amino Sugars by Using Chloroformamidinium Reagent in Water

Noguchi, Masato; Tanaka, Tomonari; Gyakushi, Hidetoshi; Kobayashi, Atsushi; Shoda, Shin Ichiro

doi:10.1021/jo8024708

Cited by 166 publications

(118 citation statements)

References 29 publications

(14 reference statements)

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“…pNPdi-or trisaccharides with various core structures of mucin-type oligosaccharides were chemically synthesized (22); the other pNP-glycosides including GalNAc␣1-pNP were from SigmaAldrich. 4,6-Dimethoxy-1,3,5-triazin-2-yl ␣-N-acetylgalactosaminide (GalNAc␣1-DMT) was synthesized by stirring 4-(4,6-dimethoxy-1,3,5-triazin-2-yl)-4-methylmorpholinium chloride (Tokyo Chemical Industry, Japan), 2,6-lutidine (Nacalai Tesque, Japan), and GalNAc in water at room temperature as described (23,24) and then purified by silica gel 60 (0.063-0.200 mm) column chromatography (1 ϫ 20 cm) with ethyl acetate/methanol (7:1, v/v) as an eluent. Hydrolyses of substrates were also monitored by silica gel TLC (Merck 5553, Germany) with 1-butanol/acetic acid/water (2:1:1, v/v/v) as a developing solvent, and the released sugars were visualized using diphenylamine/aniline/phosphoric acid (25).…”

Section: Methodsmentioning

confidence: 99%

α-N-Acetylgalactosaminidase from Infant-associated Bifidobacteria Belonging to Novel Glycoside Hydrolase Family 129 Is Implicated in Alternative Mucin Degradation Pathway

Kiyohara

Nakatomi

Kurihara

et al. 2012

Journal of Biological Chemistry

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Background:The degradation pathway of the intestinal mucin by bifidobacteria is poorly understood. Results: A novel ␣-N-acetylgalactosaminidase, NagBb, was identified from Bifidobacterium bifidum JCM 1254. Conclusion: NagBb might be involved in intracellular degradation of Tn antigen (GalNAc␣1-Ser/Thr). Significance: NagBb represents a novel glycoside hydrolase family 129 in the CAZy database.

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Section: Methodsmentioning

confidence: 99%

α-N-Acetylgalactosaminidase from Infant-associated Bifidobacteria Belonging to Novel Glycoside Hydrolase Family 129 Is Implicated in Alternative Mucin Degradation Pathway

Kiyohara

Nakatomi

Kurihara

et al. 2012

Journal of Biological Chemistry

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“…Recently, the enzymatic synthesis of glycoproteins has also been demonstrated by means of an oxazoline oligosaccharide donor. 51 This method also improved the synthesis of homogeneous glycoproteins. 52 These synthetic methods complement the biological preparation method and open an avenue to synthesizing homogeneous glycoproteins, such as a total synthesis of natural products of small or middle molecular size.…”

Section: ¼ 14)mentioning

confidence: 98%

Studies on the Precise Chemical Synthesis of Human Glycoproteins

Kajihara¹

2015

Bulletin of the Chemical Society of Japan

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Our research group demonstrated the semi-synthesis of complex-type biantennary sialyloligosaccharide-library by means of branch-specific glycosidase and several sialyltransferase reactions toward complex-type H 2 N-Asn-(biantennary compex-type sialyloligosaccharide)-COOH isolated from egg yolk at over a gram scale. This methodology yielded 35 kinds of homogeneous complex-type oligosaccharides. Using this oligosaccharide library, an efficient Boc solid phase peptide synthesis (SPPS) of acid labile sialylglycopeptide-α-thioester was demonstrated. Our research group showed that the sialoside in which the carboxylic acid is protected with a phenacyl group is stable under strong acidic conditions, and this critical finding enabled us to demonstrate the first Boc-SPPS for the synthesis of a sialylglycopeptide-α-thioester. Using both a synthetic method of sialylglycopeptide-α-thioester and native chemical ligation (NCL), our research group synthesized several glycoproteins such as chemokine MCP-3, three kinds of erythropoietin analogues, and interferon-ß. Our research group also demonstrated a unique synthesis that was an intentional synthesis of homogeneous misfolded glycoproteins bearing M9-high-mannose-type oligosaccharide. This unique synthetic misfolded-glycoprotein is useful for the purpose of uncovering the mechanism of molecular recognition in glycoprotein quality control (GQC) in the endoplasmic reticulum (ER). This account discusses the function of the oligosaccharides of glycoproteins based on our research findings.

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“…5C). The only minor (Ͻ5%) contamination could be attributed to a triantennary N-glycan isomer that contains an isomeric ␣1,3-galacto- (6) was converted into the corresponding glycan oxazolines (7) in a single step by treatment with an excess of 2-chloro-1,3-dimethylimidazolinium chloride and triethylamine in water, following the procedures reported previously (37,57,72). The reaction was monitored by HPAEC-PAD, and the product formation was found to be essentially quantitative (Fig.…”

Section: Generation and Characterization Of Glycosynthase Mutants Of mentioning

confidence: 99%

Endo-F3 Glycosynthase Mutants Enable Chemoenzymatic Synthesis of Core-fucosylated Triantennary Complex Type Glycopeptides and Glycoproteins

Giddens

Lomino

Amin

et al. 2016

Journal of Biological Chemistry

115

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Chemoenzymatic synthesis is emerging as a promising approach to the synthesis of homogeneous glycopeptides and glycoproteins highly demanded for functional glycomics studies, but its generality relies on the availability of a range of enzymes with high catalytic efficiency and well defined substrate specificity. We describe in this paper the discovery of glycosynthase mutants derived from Elizabethkingia meningoseptica endoglycosidase F3 (Endo-F3) of the GH18 family, which are devoid of the inherent hydrolytic activity but are able to take glycan oxazolines for transglycosylation. Notably, the Endo-F3 D165A and D165Q mutants demonstrated high acceptor substrate specificity toward ␣1,6-fucosyl-GlcNAc-Asn or ␣1, 6-fucosyl-GlcNAc-polypeptide in transglycosylation, enabling a highly convergent synthesis of core-fucosylated, complex CD52 glycopeptide antigen. The Endo-F3 mutants were able to use both bi-and triantennary glycan oxazolines as substrates for transglycosylation, in contrast to previously reported endoglycosidases derived from Endo-S, Endo-M, Endo-D, and Endo-A mutants that could not recognize triantennary N-glycans. Using rituximab as a model system, we have further demonstrated that the Endo-F3 mutants are highly efficient for glycosylation remodeling of monoclonal antibodies to produce homogeneous intact antibody glycoforms. Interestingly, the new triantennary glycan glycoform of antibody showed much higher affinity for galectin-3 than that of the commercial antibody. The Endo-F3 mutants represent the first endoglycosidase-based glycosynthases capable of transferring triantennary complex N-glycans, which would be very useful for glycoprotein synthesis and glycosylation remodeling of antibodies.Protein glycosylation is one of the most prevalent posttranslational modifications, found in almost all living organisms ranging from bacteria to eukaryotes (1). Glycosylation can profoundly affect a protein's intrinsic properties, such as folding, stability, intracellular trafficking, and immunogenicity. In addition, the oligosaccharide components of glycoproteins can participate directly in a number of important biological recognition processes, including cell adhesion, signaling, hostpathogen interactions, and immune responses (2-8). It is well documented that subtle changes in glycosylation can lead to a significant impact on the biological functions and, in the case of therapeutic glycoproteins, such as monoclonal antibodies, the in vivo stability and therapeutic efficacy (7, 9 -12). Natural and recombinant glycoproteins are usually produced as mixtures of glycoforms that differ only in the structures of pendant glycans, from which pure glycoforms are extremely difficult to isolate by current chromatographic techniques. As a result, synthetic homogeneous glycopeptides and glycoproteins emerge as indispensable tools for functional studies and for drug/vaccine discoveries. Many elegant chemical and biochemical strategies have been explored for making homogeneous glycoproteins and mimics, including total chemic...

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Efficient Synthesis of Sugar Oxazolines from Unprotected N-Acetyl-2-amino Sugars by Using Chloroformamidinium Reagent in Water

Cited by 166 publications

References 29 publications

α-N-Acetylgalactosaminidase from Infant-associated Bifidobacteria Belonging to Novel Glycoside Hydrolase Family 129 Is Implicated in Alternative Mucin Degradation Pathway

α-N-Acetylgalactosaminidase from Infant-associated Bifidobacteria Belonging to Novel Glycoside Hydrolase Family 129 Is Implicated in Alternative Mucin Degradation Pathway

Studies on the Precise Chemical Synthesis of Human Glycoproteins

Endo-F3 Glycosynthase Mutants Enable Chemoenzymatic Synthesis of Core-fucosylated Triantennary Complex Type Glycopeptides and Glycoproteins

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