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Synthesis of the Highly Glycosylated Hydrophilic Motif of Extensins
Author(s) -
Ishiwata Akihiro,
Kaeothip Sophon,
Takeda Yoichi,
Ito Yukishige
Publication year - 2014
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201404904
Subject(s) - pentapeptide repeat , stereochemistry , residue (chemistry) , hydroxylation , chemistry , stereoselectivity , intramolecular force , serine , glycosylation , peptide , proline , biochemistry , amino acid , enzyme , catalysis
Abstract Extensin, the structural motif of plant extracellular matrix proteins, possesses a unique highly glycosylated, hydrophilic, and repeating Ser 1 Hyp 4 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(Galp 1 )‐Hyp(Araf 4 )‐Hyp(Araf 4 )‐Hyp(Araf 3 )‐Hyp(Araf 1 ). The synthesis has been completed by the application of 2‐(naphthyl)methylether‐mediated intramolecular aglycon delivery to the stereoselective construction of the Ser(Galp 1 ) and Hyp(Araf n ) fragments as the key step, as well as Fmoc solid‐phase peptide synthesis for the backbone pentapeptide.