The detection and annotation of posttranslationally modified proteins in complex samples
has benefited greatly from the ability to chemically synthesize and characterize model
compounds harboring the modification of interest. To explore the signaling role of
protein pyrophosphorylation, a recently discovered modification mediated by the inositol
pyrophosphate messengers, our group has developed a robust method to incorporate pyrophosphate
residues into peptide sequences. We highlight several examples from the literature
that inspired our chemical approach and discuss future applications of our orthogonal
pyrophosphorylation strategy.
Key words
bioorganic chemistry - pyrophosphorylation - peptides - phosphorimidazolide - phosphorylation
- chemoselectivity
