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

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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.

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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14-3-3 Proteins
Phosphopeptides
Amino acids
Substitution reactions
Proteins
Phosphoserine
Amino Acids
Proline
Thermodynamics

Cite this

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

In: Chemical Communications, Vol. 55, No. 98, 05.12.2019, p. 14809-14812.

Research output: Contribution to journalArticleAcademicpeer-review

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AU - Thijssen, Vito

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AU - Ottmann, Christian

AU - Milroy, Lech-Gustav

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