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Toward Fully Synthetic N ‐Linked Glycoproteins
Author(s) -
Miller Justin S.,
Dudkin Vadim Y.,
Lyon Gholson J.,
Muir Tom W.,
Danishefsky Samuel J.
Publication year - 2003
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.200390131
Subject(s) - glycopeptide , acylation , glycan , amination , residue (chemistry) , chemistry , native chemical ligation , asparagine , peptide , combinatorial chemistry , glycoprotein , yield (engineering) , homogeneous , reductive amination , biochemistry , amino acid , chemical synthesis , in vitro , mathematics , materials science , antibiotics , combinatorics , metallurgy , catalysis
Substantial quantities of fully synthetic, homogeneous, N ‐linked glycopeptides may be accessed by a highly convergent and flexible protocol. Only four transformations are required to generate naturally linked glycopeptides in high yield. Amination of a free glycan is followed by acylation with an asparagine residue of a peptide and Fmoc deprotection; native chemical ligation completes the puzzle to afford N ‐linked glycopeptides (see scheme). Fmoc=9‐fluorenylmethoxycarbonyl.