Chemoenzymatic synthesis of diverse asparagine-linked α-(2,3)-sialyloligosaccharides

Fukae, Kazuhiro; Yamamoto, Naoki; Hatakeyama, Yuri; Kajihara, Yasuhiro

doi:10.1023/b:glyc.0000045096.89408.50

Cited by 11 publications

(6 citation statements)

References 8 publications

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“…For the preparation of glycosyl asparagine thioacid 3 , asparagine with a homogeneous complex-type biantennary sialyloligosaccharide can be isolated from egg yolk or egg powder on a gram scale. − These glycans are now easily converted into diverse structures by glycosidases and glycosyltransferases. , In particular, the Boons group developed sophisticated enzymatic synthesis of many asymmetric N-glycans . These methodologies will serve to prepare many glycoforms.…”

Section: Discussionmentioning

confidence: 99%

Glycoprotein Semisynthesis by Chemical Insertion of Glycosyl Asparagine Using a Bifunctional Thioacid-Mediated Strategy

et al. 2021

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Glycosylation is a major modification of secreted and cell surface proteins, and the resultant glycans show considerable heterogeneity in their structures. To understand the biological processes arising from each glycoform, the preparation of homogeneous glycoproteins is essential for extensive biological experiments. To establish a more robust and rapid synthetic route for the synthesis of homogeneous glycoproteins, we studied several key reactions based on amino thioacids. We found that diacyl disulfide coupling (DDC) formed with glycosyl asparagine thioacid and peptide thioacid yielded glycopeptides. This efficient coupling reaction enabled us to develop a new glycoprotein synthesis method, such as the bifunctional thioacid-mediated strategy, which can couple two peptides with the N-and C-termini of glycosyl asparagine thioacid. Previous glycoprotein synthesis methods required valuable glycosyl asparagine in the early stage and subsequent multiple glycoprotein synthesis routes, whereas the developed concept can generate glycoproteins within a few steps from peptide and glycosyl asparagine thioacid. Herein, we report the characterization of the DDC of amino thioacids and the efficient ability of glycosyl asparagine thioacid to be used for robust glycoprotein semisynthesis.

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Section: Discussionmentioning

confidence: 99%

Glycoprotein Semisynthesis by Chemical Insertion of Glycosyl Asparagine Using a Bifunctional Thioacid-Mediated Strategy

et al. 2021

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“…37 This biantennary sialyloligosaccharide 1 can be prepared from hen egg yolk on a gram scale, which is a well-established procedure. 23,39,40 Besides that, the carboxylic acid of acid labile sialic acid was protected with Pac ester in order to prevent the hydrolysis of the sialyl linkage by the self-intraacid catalyst (Fig. 2b).…”

Section: Papermentioning

confidence: 99%

Optimizing the Semisynthesis towards glycosylated interferon-β-polypeptide by utilizing bacterial protein expression and chemical modification

et al. 2022

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“…Using several different glycosidases and α-2,3-sialyltransferase enabled us to obtain an additional 11 oligosaccharide repertoire. 26 …”

Section: The Semisynthesis Of Human-type Oligosaccharidesmentioning

confidence: 99%

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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Chemoenzymatic synthesis of diverse asparagine-linked α-(2,3)-sialyloligosaccharides

Cited by 11 publications

References 8 publications

Glycoprotein Semisynthesis by Chemical Insertion of Glycosyl Asparagine Using a Bifunctional Thioacid-Mediated Strategy

Glycoprotein Semisynthesis by Chemical Insertion of Glycosyl Asparagine Using a Bifunctional Thioacid-Mediated Strategy

Optimizing the Semisynthesis towards glycosylated interferon-β-polypeptide by utilizing bacterial protein expression and chemical modification

Studies on the Precise Chemical Synthesis of Human Glycoproteins

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