Abstract
Tyrosine O-sulfation is a common protein post-translational modification that regulates many biological processes, including leukocyte adhesion and chemotaxis. Many peptides with therapeutic potential contain one or more sulfotyrosine residues. We report a one-step synthesis for Fmoc-fluorosulfated tyrosine. An efficient Fmoc-based solid-phase peptide synthetic strategy is then introduced for incorporating the fluorosulfated tyrosine residue into peptides of interest. Standard simultaneous peptide-resin cleavage and removal of the acid-labile side-chain protecting groups affords the crude peptides containing fluorosulfated tyrosine. Basic ethylene glycol, serving both as solvent and reactant, transforms the fluorosulfated tyrosine peptides into sulfotyrosine peptides in high yield.
Original language | English (US) |
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Pages (from-to) | 1835-1838 |
Number of pages | 4 |
Journal | Angewandte Chemie - International Edition |
Volume | 55 |
Issue number | 5 |
DOIs | |
State | Published - Jan 26 2016 |
All Science Journal Classification (ASJC) codes
- Catalysis
- General Chemistry