Development of ketobenzothiazole-based peptidomimetic TMPRSS13 inhibitors with low nanomolar potency

TMPRSS13, a member of the Type II Transmembrane Serine Proteases (TTSP) family, is involved in cancer progression and in respiratory virus cell entry. To date, no inhibitors have been specifically developed for this protease. In this study, a chemical library of 65 ketobenzothiazole-based peptidomimetic molecules was screened against a proteolytically active form of recombinant TMPRSS13 to identify novel inhibitors. Following an initial round of screening, subsequent synthesis of additional derivatives supported by molecular modelling revealed important molecular determinants involved in TMPRSS13 inhibition. One inhibitor, N-0430, achieved low nanomolar affinity towards TMPRSS13 activity in a cellular context. Using a SARS-CoV-2 pseudovirus cell entry model, we further demonstrated the ability of N-0430 to block TMPRSS13-dependent entry of the pseudovirus. The identified peptidomimetic inhibitors and the molecular insights into their potency gained from this study will aid in the development of specific TMPRSS13 inhibitors.

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Publication Details

Journal
Journal of Enzyme Inhibition and Medicinal Chemistry
Published
2025-02-20
DOI
https://doi.org/10.1080/14756366.2025.2466841
Citations
4
Primary Topic
Protein Tyrosine Phosphatases
Type
article
Field-Weighted Citation Impact
3.22
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article

Development of ketobenzothiazole-based peptidomimetic TMPRSS13 inhibitors with low nanomolar potency

Ulrike Froehlich, Antoine Désilets, Pierre‐Luc Boudreault, Karin List et al.
4 citations
Journal of Enzyme Inhibition and Medicinal Chemistry
Protein Tyrosine Phosphatases
3.22
article

Development of ketobenzothiazole-based peptidomimetic TMPRSS13 inhibitors with low nanomolar potency

Ulrike Froehlich, Antoine Désilets, Pierre‐Luc Boudreault, Karin List, Gabriel Lemieux, Richard Leduc, Alice Gravel-Trudeau, Alexandre Joushomme, William Champagne, Sabrina Lafrenière, Malihe Hassanzadeh, Matthieu Lepage
article en
4 citations

Abstract

TMPRSS13, a member of the Type II Transmembrane Serine Proteases (TTSP) family, is involved in cancer progression and in respiratory virus cell entry. To date, no inhibitors have been specifically developed for this protease. In this study, a chemical library of 65 ketobenzothiazole-based peptidomimetic molecules was screened against a proteolytically active form of recombinant TMPRSS13 to identify novel inhibitors. Following an initial round of screening, subsequent synthesis of additional derivatives supported by molecular modelling revealed important molecular determinants involved in TMPRSS13 inhibition. One inhibitor, N-0430, achieved low nanomolar affinity towards TMPRSS13 activity in a cellular context. Using a SARS-CoV-2 pseudovirus cell entry model, we further demonstrated the ability of N-0430 to block TMPRSS13-dependent entry of the pseudovirus. The identified peptidomimetic inhibitors and the molecular insights into their potency gained from this study will aid in the development of specific TMPRSS13 inhibitors.

Journal of Enzyme Inhibition and Medicinal ChemistryVol. 40(1)
Université de Sherbrooke (CA), Wayne State University (US)
Openalex Percentile: Top 9%
Protein Tyrosine Phosphatases
3.22
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