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  • Title: N-->O-Acyl shift in Fmoc-based synthesis of phosphopeptides.
    Author: Eberhard H, Seitz O.
    Journal: Org Biomol Chem; 2008 Apr 21; 6(8):1349-55. PubMed ID: 18385841.
    Abstract:
    Synthetic phosphopeptides are frequently used as chemical probes to explore protein-protein interactions involved in cellular signal transduction. Most commonly, the solid-phase synthesis of phosphotyrosine-containing peptides is performed by applying the Fmoc-strategy and N-Fmoc-protected tyrosine derivatives bearing acid-labile phospho protecting groups. We observed a side-reaction, the isomerisation at threonine, which furnishes depsipeptides. It is shown that the rate of N-->O-acyl migration depends on the sequence context. Depsipeptides were formed most rapidly when the phosphotyrosine was located in the +2 position. Furthermore, different phosphotyrosine building blocks were compared and a suitable method that provides phosphopeptides in enhanced purity and yield is suggested.
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