Article: Encouraging progress in the ω-aspartylation of complex oligosaccharides as a general route to β-N-linked glycopolypeptides

File Download
  • No File Attached
Links for fulltext
(May Require Subscription)
Supplementary
  • Basic View
  • Metadata View
  • XML View
TitleEncouraging progress in the ω-aspartylation of complex oligosaccharides as a general route to β-N-linked glycopolypeptides
AuthorsWang, P1
Li, X1
Zhu, J1
Chen, J1
Yuan, Y1
Wu, X1
Danishefsky, SJ1 2
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
2011 Impact Factor: 9.907
2011 SCImago Journal Rankings: 1.117
DOIhttp://dx.doi.org/10.1021/ja110115a
ReferencesReferences in Scopus
DC Field
Value
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
2011 Impact Factor: 9.907
2011 SCImago Journal Rankings: 1.117
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
Author Affiliations
  1. Memorial Sloan-Kettering Cancer Center
  2. Columbia University in the City of New York