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

Sebastian A Andrei, Vito Thijssen, Luc Brunsveld, Christian Ottmann, Lech-Gustav Milroy

Research output: Contribution to journalArticleAcademicpeer-review

2 Citations (Scopus)
23 Downloads (Pure)

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.

Original languageEnglish
Pages (from-to)14809-14812
Number of pages4
JournalChemical Communications
Volume55
Issue number98
DOIs
Publication statusPublished - 5 Dec 2019

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