Molecular design of glycoprotein mimetics: Glycoblotting by engineered proteins with an oxylamino-functionalized amino acid residue

Naoki Matsubara, Kei Oiwa, Takahiro Hohsaka, Reiko Sadamoto, Kenichi Niikura, Norio Fukuhara, Akio Takimoto, Hirosato Kondo, Shin Ichiro Nishimura

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21 Citations (Scopus)

Abstract

The general and efficient method for the site-directed glycosylation of proteins is a key step in order to understand the biological importance of the carbohydrate chains of proteins and to control functional roles of the engineered glycoproteins in terms of the development of improved glycoprotein therapeutics. We have developed a novel method for site-directed glycosylation of proteins based on chemoselective blotting of common reducing sugars by genetically encoded proteins. The oxylamino-functionalized L-homoserine residues, 2-amino-4-O-(N-methylaminooxy) butanoic acid and 2-amino-4-aminooxy butanoic acid, were efficiently incorporated into proteins by using the four-base codon/anticodon pair strategy in Escherichia coli in vitro translation. Direct and chemoselective coupling between unmodified simple sugars and N-methylaminooxy group displayed on the engineered streptavidin allowed for the combinatorial synthesis of novel glycoprotein mimetics.

Original languageEnglish
Pages (from-to)6974-6981
Number of pages8
JournalChemistry - A European Journal
Volume11
Issue number23
DOIs
Publication statusPublished - Nov 18 2005
Externally publishedYes

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All Science Journal Classification (ASJC) codes

  • Catalysis
  • Organic Chemistry

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