Toward fully synthetic N-linked glycoproteins Journal Article
| Authors: | Miller, J. S.; Dudkin, V. Y.; Lyon, G. J.; Muir, T. W.; Danishefsky, S. J. |
| Article Title: | Toward fully synthetic N-linked glycoproteins |
| Abstract: | 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. |
| Keywords: | protein conformation; protein domain; mass spectrometry; proteins; protein analysis; carboxy terminal sequence; amino acid sequence; molecular sequence data; protein purification; protein synthesis; glycosylation; peptides; high performance liquid chromatography; amination; polysaccharides; oligopeptides; molecular weight; glycoproteins; glycoprotein; aspartic acid; synthesis (chemical); carbohydrate sequence; carbohydrates; glycopeptides; proton nuclear magnetic resonance; carboxylic acid; carbon nuclear magnetic resonance; oligosaccharide; acylation; polypeptide; oligosaccharides; synthetic methods; article; fluorine compounds; carbonic acid derivative; freeze drying |
| Journal Title: | Angewandte Chemie - International Edition |
| Volume: | 42 |
| Issue: | 4 |
| ISSN: | 1433-7851 |
| Publisher: | Wiley Blackwell |
| Date Published: | 2003-01-27 |
| Start Page: | 431 |
| End Page: | 434 |
| Language: | English |
| DOI: | 10.1002/anie.200390131 |
| PUBMED: | 12569509 |
| PROVIDER: | scopus |
| DOI/URL: | |
| Notes: | Export Date: 12 September 2014 -- Source: Scopus |
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