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A biomimetic electrostatic assistance for guiding and promoting N-terminal protein chemical modification

Author

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  • Nathalie Ollivier

    (Univ. Lille, CNRS, Inserm, CHU Lille, Institut Pasteur de Lille, U1019 - UMR 9017; Center for Infection and Immunity of Lille)

  • Magalie Sénéchal

    (Univ. Lille, CNRS, Inserm, CHU Lille, Institut Pasteur de Lille, U1019 - UMR 9017; Center for Infection and Immunity of Lille)

  • Rémi Desmet

    (Univ. Lille, CNRS, Inserm, CHU Lille, Institut Pasteur de Lille, U1019 - UMR 9017; Center for Infection and Immunity of Lille)

  • Benoît Snella

    (Univ. Lille, CNRS, Inserm, CHU Lille, Institut Pasteur de Lille, U1019 - UMR 9017; Center for Infection and Immunity of Lille)

  • Vangelis Agouridas

    (Univ. Lille, CNRS, Inserm, CHU Lille, Institut Pasteur de Lille, U1019 - UMR 9017; Center for Infection and Immunity of Lille
    Centrale Lille)

  • Oleg Melnyk

    (Univ. Lille, CNRS, Inserm, CHU Lille, Institut Pasteur de Lille, U1019 - UMR 9017; Center for Infection and Immunity of Lille)

Abstract

The modification of protein electrostatics by phosphorylation is a mechanism used by cells to promote the association of proteins with other biomolecules. In this work, we show that introducing negatively charged phosphoserines in a reactant is a powerful means for directing and accelerating the chemical modification of proteins equipped with oppositely charged arginines. While the extra charged amino acid residues induce no detectable affinity between the reactants, they bring site-selectivity to a reaction that is otherwise devoid of such a property. They also enable rate accelerations of four orders of magnitude in some cases, thereby permitting chemical processes to proceed at the protein level in the low micromolar range, using reactions that are normally too slow to be useful in such dilute conditions.

Suggested Citation

  • Nathalie Ollivier & Magalie Sénéchal & Rémi Desmet & Benoît Snella & Vangelis Agouridas & Oleg Melnyk, 2022. "A biomimetic electrostatic assistance for guiding and promoting N-terminal protein chemical modification," Nature Communications, Nature, vol. 13(1), pages 1-10, December.
    • Handle: RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-022-34392-5
    DOI: 10.1038/s41467-022-34392-5
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    References listed on IDEAS

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    1. Manuel C. Martos-Maldonado & Christian T. Hjuler & Kasper K. Sørensen & Mikkel B. Thygesen & Jakob E. Rasmussen & Klaus Villadsen & Søren R. Midtgaard & Stefan Kol & Sanne Schoffelen & Knud J. Jensen, 2018. "Selective N-terminal acylation of peptides and proteins with a Gly-His tag sequence," Nature Communications, Nature, vol. 9(1), pages 1-13, December.
    2. Vincent Diemer & Nathalie Ollivier & Bérénice Leclercq & Hervé Drobecq & Jérôme Vicogne & Vangelis Agouridas & Oleg Melnyk, 2020. "A cysteine selenosulfide redox switch for protein chemical synthesis," Nature Communications, Nature, vol. 11(1), pages 1-14, December.
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    1. Kazuki Yamamoto & Toyotaka Sato & Aili Hao & Kenta Asao & Rintaro Kaguchi & Shintaro Kusaka & Radhakrishnam Raju Ruddarraju & Daichi Kazamori & Kiki Seo & Satoshi Takahashi & Motohiro Horiuchi & Shin-, 2024. "Development of a natural product optimization strategy for inhibitors against MraY, a promising antibacterial target," Nature Communications, Nature, vol. 15(1), pages 1-15, December.

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