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Issue 27, 2018
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Pyrophosphorylation via selective phosphoprotein derivatization

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Abstract

An important step in elucidating the function of protein post-translational modifications (PTMs) is gaining access to site-specifically modified, homogeneous samples for biochemical characterization. Protein pyrophosphorylation is a poorly characterized PTM, and here a chemical approach to obtain pyrophosphoproteins is reported. Photo-labile phosphorimidazolide reagents were developed for selective pyrophosphorylation, affinity-capture, and release of pyrophosphoproteins. Kinetic analysis of the reaction revealed rate constants between 9.2 × 10−3 to 0.58 M−1 s−1, as well as a striking proclivity of the phosphorimidazolides to preferentially react with phosphate monoesters over other nucleophilic side chains. Besides enabling the characterization of pyrophosphorylation on protein function, this work highlights the utility of phosphoryl groups as handles for selective protein modification for a variety of applications, such as phosphoprotein bioconjugation and enrichment.

Graphical abstract: Pyrophosphorylation via selective phosphoprotein derivatization

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Publication details

The article was received on 15 Mar 2018, accepted on 08 Jun 2018 and first published on 12 Jun 2018


Article type: Edge Article
DOI: 10.1039/C8SC01233D
Citation: Chem. Sci., 2018,9, 5929-5936
  • Open access: Creative Commons BY-NC license
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    Pyrophosphorylation via selective phosphoprotein derivatization

    Alan M. Marmelstein, J. A. M. Morgan, M. Penkert, D. T. Rogerson, J. W. Chin, E. Krause and D. Fiedler, Chem. Sci., 2018, 9, 5929
    DOI: 10.1039/C8SC01233D

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