Homoserine as an Aspartic Acid Precursor for Synthesis of Proteoglycan Glycopeptide Containing Aspartic Acid and a Sulfated Glycan Chain

J Org Chem. 2016 Dec 2;81(23):12052-12059. doi: 10.1021/acs.joc.6b02441. Epub 2016 Nov 10.

Abstract

Among many hurdles in synthesizing proteoglycan glycopeptides, one challenge is the incorporation of aspartic acid in the peptide backbone and acid sensitive O-sulfated glycan chains. To overcome this, a new strategy was developed utilizing homoserine as an aspartic acid precursor. The conversion of homoserine to aspartic acid in the glycopeptide was successfully accomplished by late stage oxidation using (2,2,6,6-tetramethyl-piperidin-1-yl)oxyl (TEMPO) and bis(acetoxy)iodobenzene (BAIB). This is the first time that a glycopeptide containing aspartic acid and an O-sulfated glycan was synthesized.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Aspartic Acid / chemistry*
  • Carbohydrate Sequence
  • Carbon-13 Magnetic Resonance Spectroscopy
  • Glycopeptides / chemical synthesis*
  • Glycopeptides / chemistry
  • Homoserine / chemistry*
  • Mass Spectrometry
  • Polysaccharides / chemistry*
  • Proteoglycans / chemistry*
  • Proton Magnetic Resonance Spectroscopy
  • Solid-Phase Synthesis Techniques
  • Sulfates / chemistry

Substances

  • Glycopeptides
  • Polysaccharides
  • Proteoglycans
  • Sulfates
  • Aspartic Acid
  • Homoserine