Fragment-Based Covalent Targeting of Lysines at the Allosteric Latch Site of SHP2

Abstract Covalent mechanism of action is a powerful way to modulate challenging drug targets. Here, we present a streamlined workflow that combines covalent fragment screening (electrophile first approach) and ligand-first strategy to identify covalent inhibitors targeting lysine residues in the allosteric latch site of SHP2 phosphatase. Supported by complementary computational and experimental analyses, this strategy enabled us to identify the first potent cell active allosteric covalent inhibitors acting at this site. Demonstrating the covalent tractability of the latch site opens further avenues for future optimization and therapeutic exploration of high-value allosteric SHP2 inhibitors.

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Publication Details

Journal
Journal of Medicinal Chemistry
Published
2026-09-18
DOI
https://doi.org/10.1021/acs.jmedchem.6c01030
Primary Topic
Protein Tyrosine Phosphatases
Type
article
Field-Weighted Citation Impact
0.00

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article

Fragment-Based Covalent Targeting of Lysines at the Allosteric Latch Site of SHP2

Péter Ábrányi‐Balogh, Levente Kollár, György M. Keserű, Tı́mea Imre et al.
Journal of Medicinal Chemistry
Protein Tyrosine Phosphatases
article

Fragment-Based Covalent Targeting of Lysines at the Allosteric Latch Site of SHP2

Péter Ábrányi‐Balogh, Levente Kollár, György M. Keserű, Tı́mea Imre, Renáta Szabó, Noémi Csorba, V. di Lorenzo, Marc Nazaré, Levente Mihalovits, Nina‐Louisa Efrém, József Tóvári, Ivan Ranđelović, József Simon, Tibor Viktor Szalai, Yvette Roske, Oliver Daumke, Krisztina Balázs
article en

Abstract

Abstract Covalent mechanism of action is a powerful way to modulate challenging drug targets. Here, we present a streamlined workflow that combines covalent fragment screening (electrophile first approach) and ligand-first strategy to identify covalent inhibitors targeting lysine residues in the allosteric latch site of SHP2 phosphatase. Supported by complementary computational and experimental analyses, this strategy enabled us to identify the first potent cell active allosteric covalent inhibitors acting at this site. Demonstrating the covalent tractability of the latch site opens further avenues for future optimization and therapeutic exploration of high-value allosteric SHP2 inhibitors.

Journal of Medicinal Chemistry
Karlsruhe Institute of Technology (DE), Bielefeld University (DE), Hochschule Bielefeld (DE), Max Delbrück Center (DE), Budapest University of Technology and Economics (HU), Leibniz-Forschungsinstitut für Molekulare Pharmakologie (DE), National Institute of Oncology (HU), HUN-REN Research Centre for Natural Sciences (HU)
Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung, Magyar Tudományos Akadémia, Nemzeti Kutatási Fejlesztési és Innovációs Hivatal
Good health and well-being
Openalex Percentile: Top 18%
Protein Tyrosine Phosphatases
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