Mature homogeneous erythropoietin building blocks by chemical synthesis: the EPO 22–37 glycopeptide domain presenting the full N-linked dodecasaccharide

Wu, Bin; Chen, Gong; Chen, Jiehao; Hua, Zihao; Wan, Qian; Ranganathan, Krishnakumar

doi:10.1016/j.tetlet.2006.09.050

Cited by 29 publications

(29 citation statements)

References 26 publications

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“…The approach of EPO(78-87) glycopeptide synthesis used here had already been charted,1,16 but the implementation was now modified and systematically optimized to avoid undesired aspartimide formation. The other issue is that of appropriate differentiation of the C-terminus of the EPO(78-87) glycopeptide and the EPO(88-113) peptide.…”

Section: Resultsmentioning

confidence: 99%

Toward Homogeneous Erythropoietin: Non-NCL-Based Chemical Synthesis of the Gln⁷⁸−Arg¹⁶⁶ Glycopeptide Domain

et al. 2009

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Single erythropoietin (EPO) glycoforms with defined mature oligosaccharide structures and amino acid sequences are essential to elucidate the molecular mechanisms by which carbohydrates exert various physiological and metabolic functions and to explore the possible links between carbohydrates and the prevention or management of diseases. To demonstrate that it is possible to generate EPO even without recourse to cysteine-based NCL, a concise synthesis of the partially-protected EPO fragment (78-166) bearing fully mature N- and O-glycans is described.

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Section: Resultsmentioning

confidence: 99%

Toward Homogeneous Erythropoietin: Non-NCL-Based Chemical Synthesis of the Gln⁷⁸−Arg¹⁶⁶ Glycopeptide Domain

et al. 2009

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“…[53] In beiden Fällen können die b-Disulfidester als "Thioester-Vorstufen" angesehen werden, die in reiterativen Reaktionen mehrerer Peptidfragmente eingesetzt werden können (weitere Strategien werden in Abschnitt 7 diskutiert). [55,56] Diese Verbindungen wurden auch auf die Synthese cyclischer Peptide [57] und Glycopeptide [58] sowie auf Peptidligationen an cysteinfreien Verknüpfungsstellen angewendet (siehe Abschnitt 3.3.4). In einem verwandten Prozess kann der Einfangschritt eines Thiolperthioesterderivats bei noch niedrigerem pH ausgeführt werden (Schema 5 C).…”

Section: Reaktionsbedingungen Für Die Ncl Und Mechanistische Aspekteunclassified

Chemoselektive Ligations‐ und Modifikationsstrategien für Peptide und Proteine

2008

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Die Untersuchung biologischer Fragestellungen mit chemischen Methoden wird meist als “Chemische Biologie” bezeichnet und setzt voraus, dass biologisch relevante Makromoleküle, wie Peptide und Proteine, chemisch zugänglich sind. Auf der Festphasensynthese von Peptiden aufbauend wurden viele chemoselektive Ligations‐ und Modifikationstechniken zur Verknüpfung synthetischer Peptide oder funktionaler Einheiten zu größeren synthetischen, biologisch relevanten Makromolekülen entwickelt. Dieser Aufsatz fasst die aktuellen Entwicklungen auf dem Gebiet der chemoselektiven Ligations‐ und Modifikationsstrategien zusammen und illustriert ihre Anwendbarkeit an Beispielen aus der chemischen Totalsynthese von Proteinen bis hin zur Semisynthese natürlicher modifizierter Proteine.

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“…The invention of removable thiol auxiliaries [27,[32][33][34][35] has expanded the sequence repertoire that is accessible to NCL, and recently the new methods have been applied to synthesis of full-length glycoproteins [36] or fragments thereof. [37,38] However, ligation junction sequence dependence remains a serious issue, as these auxiliary-based systems rely on an amine that is less nucleophilic and more hindered than a native peptide's N-terminal primary amine. Thus, these ligations are generally slower and proceed in lower yields, and with more racemization, than traditional cysteine-based NCL ligations.…”

Section: Introductionmentioning

confidence: 99%

Enzymes for Glycoprotein Synthesis

Wong¹

2009

Chimia

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More than 90% of human proteins are glycosylated and since protein glycosylation is understood to play a role in folding, trafficking, stability, immunogenicity, and function there is a need to generate pure protein glycoforms. Pure single protein glycoforms are difficult to obtain because the cellular machinary produces complex mixtures for any given protein. In this article an overview is given of various approaches used to generate specific single glycoforms of proteins, studies of the role of glycosylation in protein stability and function, and the imaging and identification of new glycoproteins related to cancer.

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Mature homogeneous erythropoietin building blocks by chemical synthesis: the EPO 22–37 glycopeptide domain presenting the full N-linked dodecasaccharide

Cited by 29 publications

References 26 publications

Toward Homogeneous Erythropoietin: Non-NCL-Based Chemical Synthesis of the Gln⁷⁸−Arg¹⁶⁶ Glycopeptide Domain

Toward Homogeneous Erythropoietin: Non-NCL-Based Chemical Synthesis of the Gln⁷⁸−Arg¹⁶⁶ Glycopeptide Domain

Chemoselektive Ligations‐ und Modifikationsstrategien für Peptide und Proteine

Enzymes for Glycoprotein Synthesis

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Mature homogeneous erythropoietin building blocks by chemical synthesis: the EPO 22–37 glycopeptide domain presenting the full N-linked dodecasaccharide

Cited by 29 publications

References 26 publications

Toward Homogeneous Erythropoietin: Non-NCL-Based Chemical Synthesis of the Gln78−Arg166 Glycopeptide Domain

Toward Homogeneous Erythropoietin: Non-NCL-Based Chemical Synthesis of the Gln78−Arg166 Glycopeptide Domain

Chemoselektive Ligations‐ und Modifikationsstrategien für Peptide und Proteine

Enzymes for Glycoprotein Synthesis

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Product

Resources

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Toward Homogeneous Erythropoietin: Non-NCL-Based Chemical Synthesis of the Gln⁷⁸−Arg¹⁶⁶ Glycopeptide Domain

Toward Homogeneous Erythropoietin: Non-NCL-Based Chemical Synthesis of the Gln⁷⁸−Arg¹⁶⁶ Glycopeptide Domain