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Chemoenzymatic synthesis of PSGL-1 glycopeptides: sulfation on tyrosine affects glycosyltransferase-catalyzed synthesis of the O-glycan

Academic Article
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Overview

related to degree

  • Koeller, Kathryn, Ph.D. in Chemistry, Scripps Research 1996 - 2000

authors

  • Koeller, Kathryn
  • Smith, M. E. B.
  • Wong, Chi-Huey

publication date

  • 2000

journal

  • Bioorganic & Medicinal Chemistry  Journal

abstract

  • PSGL-1 is the primary glycoprotein ligand for P-selectin during the inflammatory response. Interestingly, the N-terminal sequence, containing both a site of tyrosine sulfation and an O-glycan, has been shown to bind to P-selectin with an affinity similar to full-length PSGL-1. To further characterize this system, the synthesis of glycopeptides from PSGL-1 was undertaken. The synthesis involved both solution- and solid-phase synthesis, as well as enzymatic transformations. During the synthesis, notable reactivity differences of the glycosyltransferases toward sulfated and unsulfated versions of the same glycopeptides were observed.

subject areas

  • Amino Acid Sequence
  • Carbohydrate Sequence
  • Catalysis
  • Glycosyltransferases
  • Mass Spectrometry
  • Membrane Glycoproteins
  • Molecular Sequence Data
  • Nuclear Magnetic Resonance, Biomolecular
  • Peptides
  • Polysaccharides
  • Sulfates
  • Tyrosine
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Identity

International Standard Serial Number (ISSN)

  • 0968-0896

Digital Object Identifier (DOI)

  • 10.1016/s0968-0896(00)00041-9

PubMed ID

  • 10882013
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Additional Document Info

start page

  • 1017

end page

  • 1025

volume

  • 8

issue

  • 5

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