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Issue 98, 2019
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A study on the effect of synthetic α-to-β3-amino acid mutations on the binding of phosphopeptides to 14-3-3 proteins

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Abstract

Here we describe the synthesis of a series of α,β-phosphopeptides, based on the phosphoepitope site on YAP1 (yes-associated protein 1), and the biochemical, biophysical and structural characterization of their binding to 14-3-3 proteins. The impact of systematic mono- and di-substitution of α → β3 amino acid residues around the phosphoserine residue are discussed. Our results confirm the important role played by the +2 proline residue in the thermodynamics and structure of the phosphoepitope/14-3-3 interaction.

Graphical abstract: A study on the effect of synthetic α-to-β3-amino acid mutations on the binding of phosphopeptides to 14-3-3 proteins

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Publication details

The article was received on 14 Oct 2019, accepted on 15 Nov 2019 and first published on 15 Nov 2019


Article type: Communication
DOI: 10.1039/C9CC07982C
Chem. Commun., 2019,55, 14809-14812
  • Open access: Creative Commons BY-NC license
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    A study on the effect of synthetic α-to-β3-amino acid mutations on the binding of phosphopeptides to 14-3-3 proteins

    S. A. Andrei, V. Thijssen, L. Brunsveld, C. Ottmann and L. Milroy, Chem. Commun., 2019, 55, 14809
    DOI: 10.1039/C9CC07982C

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