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Article: Encouraging progress in the ω-aspartylation of complex oligosaccharides as a general route to β-N-linked glycopolypeptides
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TitleEncouraging progress in the ω-aspartylation of complex oligosaccharides as a general route to β-N-linked glycopolypeptides
 
AuthorsWang, P2
Li, X2
Zhu, J2
Chen, J2
Yuan, Y2
Wu, X2
Danishefsky, SJ2 1
 
Issue Date2011
 
PublisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/journals/jacsat/index.html
 
CitationJournal Of The American Chemical Society, 2011, v. 133 n. 5, p. 1597-1602 [How to Cite?]
DOI: http://dx.doi.org/10.1021/ja110115a
 
AbstractDescribed herein is a method for the joining of complex peptides to complex oligosaccharides via an N-linkage. The ω-aspartylation is conducted by coupling fully deprotected glycosylamine with a peptide containing a unique thioacid at the ω-aspartate carboxyl. In the presence of HOBT, under conditions that, in principle, allow for oxidation, complex components are combined in encouraging yields to produce structurally and stereochemically defined N-linked glycopolypeptides wherein the carbohydrate domain can be quite complex. Various mechanisms for oxidative coupling are proposed. © 2011 American Chemical Society.
 
ISSN0002-7863
2012 Impact Factor: 10.677
2012 SCImago Journal Rankings: 5.182
 
DOIhttp://dx.doi.org/10.1021/ja110115a
 
ReferencesReferences in Scopus
 
DC FieldValue
dc.contributor.authorWang, P
 
dc.contributor.authorLi, X
 
dc.contributor.authorZhu, J
 
dc.contributor.authorChen, J
 
dc.contributor.authorYuan, Y
 
dc.contributor.authorWu, X
 
dc.contributor.authorDanishefsky, SJ
 
dc.date.accessioned2012-10-08T03:19:47Z
 
dc.date.available2012-10-08T03:19:47Z
 
dc.date.issued2011
 
dc.description.abstractDescribed herein is a method for the joining of complex peptides to complex oligosaccharides via an N-linkage. The ω-aspartylation is conducted by coupling fully deprotected glycosylamine with a peptide containing a unique thioacid at the ω-aspartate carboxyl. In the presence of HOBT, under conditions that, in principle, allow for oxidation, complex components are combined in encouraging yields to produce structurally and stereochemically defined N-linked glycopolypeptides wherein the carbohydrate domain can be quite complex. Various mechanisms for oxidative coupling are proposed. © 2011 American Chemical Society.
 
dc.description.natureLink_to_subscribed_fulltext
 
dc.identifier.citationJournal Of The American Chemical Society, 2011, v. 133 n. 5, p. 1597-1602 [How to Cite?]
DOI: http://dx.doi.org/10.1021/ja110115a
 
dc.identifier.doihttp://dx.doi.org/10.1021/ja110115a
 
dc.identifier.epage1602
 
dc.identifier.issn0002-7863
2012 Impact Factor: 10.677
2012 SCImago Journal Rankings: 5.182
 
dc.identifier.issue5
 
dc.identifier.pmid21207981
 
dc.identifier.scopuseid_2-s2.0-79551711838
 
dc.identifier.spage1597
 
dc.identifier.urihttp://hdl.handle.net/10722/168506
 
dc.identifier.volume133
 
dc.languageeng
 
dc.publisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/journals/jacsat/index.html
 
dc.publisher.placeUnited States
 
dc.relation.ispartofJournal of the American Chemical Society
 
dc.relation.referencesReferences in Scopus
 
dc.subject.meshAmines - Chemistry
 
dc.subject.meshAmino Acid Sequence
 
dc.subject.meshAspartic Acid - Chemistry
 
dc.subject.meshGlycopeptides - Chemical Synthesis - Chemistry
 
dc.subject.meshNitrogen - Chemistry
 
dc.subject.meshOligosaccharides - Chemistry
 
dc.titleEncouraging progress in the ω-aspartylation of complex oligosaccharides as a general route to β-N-linked glycopolypeptides
 
dc.typeArticle
 
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<contributor.author>Yuan, Y</contributor.author>
<contributor.author>Wu, X</contributor.author>
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Author Affiliations
  1. Columbia University in the City of New York
  2. Memorial Sloan-Kettering Cancer Center