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Articles

Structural Modifications of Covalent Cathepsin S Inhibitors: Impact on Affinity, Selectivity, and Permeability

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By Mergim Meta, Collin Zimmer, Natalie Fuchs, Maximilian Johannes Zecher
| ACS Publications
Download Hi-Res ImageDownload to MS-PowerPointCite This:ACS Med. Chem. Lett. 2024, XXXX, XXX Terms & Conditions Most electronic Supporting Information files are available without a subscription to ACS Web Editions. Such files may be downloaded by article for research use (if there is a public use license linked to the relevant article, that license may permit other uses).
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Next Generation of Fluorometric Protease Assays: 7‐Nitrobenz‐2‐oxa‐1,3‐diazol‐4‐yl‐amides (NBD‐Amides) as Class‐Spanning Protease Substrates

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By Hannah Maus, Patrick Muller, Mergim Meta, Sabrina N. Hoba
| Wiley Online Library Verified
Abstract Fluorometric assays are one of the most frequently used methods in medicinal chemistry. Over the last 50 years, the reporter molecules for the detection of protease activity have evolved from first-generation colorimetric p-nitroanilides, through FRET substrates, and 7-amino-4-methyl coumarin (AMC)-based substrates. The aim of further substrate development is to increase sensitivity and reduce vulnerability to assay interferences.
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Subnanomolar Cathepsin S Inhibitors with High Selectivity: Optimizing Covalent Reversible α‐Fluorovinylsulfones and α‐Sulfonates as Potential Immunomodulators in Cancer

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By Natalie Fuchs, Mergim Meta, Bellinda Lantzberg, Matthias Bros
| Wiley Online Library Verified
Graphical Abstract Herein we present a series of covalent-reversible CatS inhibitors based on the α-fluorovinylsulfone and -sulfonate warhead, which were optimized by molecular docking and evaluated for selectivity towards off-targets CatB and CatL. The most potent inhibitor, 6 c, has subnanomolar affinity and selectivity towards cathepsins B and L, making it a promising lead for developing new immunomodulators in cancer therapy.
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