title: Synthesis of the highly glycosylated hydrophilic motif of extensins.
abstract: Extensin, the structural motif of plant extracellular matrix proteins, possesses a unique highly glycosylated, hydrophilic, and repeating Ser1Hyp4 pentapeptide unit, and has been proposed to include post-translational hydroxylation at proline residue and subsequent oligo-L-arabinosylations at all of the resultant hydroxyprolines as well as galactosylation at serine residue. Reported herein is the stereoselective synthesis of one of the highly glycosylated motifs, Ser(Galp1)-Hyp(Araf4)-Hyp(Araf4)-Hyp(Araf3)-Hyp(Araf1). The synthesis has been completed by the application of 2-(naphthyl)methylether-mediated intramolecular aglycon delivery to the stereoselective construction of the Ser(Galp1) and Hyp(Araf(n)) fragments as the key step, as well as Fmoc solid-phase peptide synthesis for the backbone pentapeptide.
authors.affiliation: Synthetic Cellular Chemistry Laboratory, RIKEN, 2-1 Hirosawa, Wako, Saitama 351-0198 (Japan). aishiwa@riken.jp.
authors.forename: Akihiro
authors.initials: A
authors.lastname: Ishiwata
authors.forename: Sophon
authors.initials: S
authors.lastname: Kaeothip
authors.forename: Yoichi
authors.initials: Y
authors.lastname: Takeda
authors.forename: Yukishige
authors.initials: Y
authors.lastname: Ito
mesh_terms: D017343:Genes, Plant; D006020:Glycopeptides; D006023:Glycoproteins / Q000235:genetics / Q000378:metabolism*; D006031:Glycosylation; D008958:Models, Molecular; D010940:Plant Proteins / Q000235:genetics / Q000378:metabolism*; D017434:Protein Structure, Tertiary; D060327:Solid-Phase Synthesis Techniques
chemical_list: D006020:Glycopeptides; D006023:Glycoproteins; D010940:Plant Proteins; C005488:extensin protein, plant
keywords: glycopeptides; proteins; solid-phase synthesis; synthetic methods