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Issue 8, 2008
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NO-Acyl shift in Fmoc-based synthesis of phosphopeptides

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Synthetic phosphopeptides are frequently used as chemical probes to explore proteinprotein 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 NO-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.

Graphical abstract: N→O-Acyl shift in Fmoc-based synthesis of phosphopeptides

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The article was received on 03 Dec 2007, accepted on 31 Jan 2008 and first published on 22 Feb 2008

Article type: Paper
DOI: 10.1039/B718568E
Citation: Org. Biomol. Chem., 2008,6, 1349-1355

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    NO-Acyl shift in Fmoc-based synthesis of phosphopeptides

    H. Eberhard and O. Seitz, Org. Biomol. Chem., 2008, 6, 1349
    DOI: 10.1039/B718568E

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