Combinatorial Optimization of Activity-Based Probes for Acyl Protein Thioesterases 1 and 2.
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ABSTRACT:
SUBMITTER: Vanhoutte R
PROVIDER: S-EPMC9290053 | biostudies-literature | 2022 Jul
REPOSITORIES: biostudies-literature
Publications
Combinatorial Optimization of Activity-Based Probes for Acyl Protein Thioesterases 1 and 2.
Vanhoutte Roeland R Verhelst Steven H L SHL
ACS medicinal chemistry letters 20220602 7
Acyl protein thioesterases hydrolyze fatty acid thioesters on cysteine residues of proteins. The two protein depalmitoylases APT1 and APT2 have a very high degree of similarity and show substantial overlap in substrate utility. Potent, selective, and cell-permeable activity-based probes are needed to study the role of these enzymes. Here, we employ solid-phase synthesis to create a library of covalent probes based on a triazole urea-reactive electrophile, leading to several potent and cell-perme ...[more]
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