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Phosphorylation of serine, threonine and tyrosine is counted among the most important posttranslational modifications that occur in organisms.
Therefore, the preparation of synthetic phosphorylated peptides is of significant interest for researchers. However, those synthetic efforts are frequently hampered by the lability of the phosphoester bond.
Here we present three phosphono-amino acid derivatives that serve as hydrolysis-stable mimics of pSer, pThr and pTyr, termed Pma (Ser), Pmab (Thr) and Pmp (Tyr). While those derivatives are suitably protected for their use in peptide synthesis using the Fmoc strategy, these protecting groups can be removed during final deprotection yielding phosphono-peptides, from which cellular phosphatases are unable to remove the phosphate group mimic. Consequently, peptides or semi-synthetic proteins that include Pma, Pmab or Pmp are valuable tools for cell-based experiments.
Exhibitor: Iris Biotech GmbH