期刊
CHEMBIOCHEM
卷 -, 期 -, 页码 -出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/cbic.202300157
关键词
activity-based probes; chemical probes; cysteine proteases; epoxysuccinate; inhibitors
Synthetic chemical probes are important tools for studying biological processes, especially in proteomic studies. Peptidyl-epoxysuccinates, derived from natural substrates, are widely used as chemical probes to investigate the activity of cysteine protease enzymes. These probes can covalently label active enzymes and have been extensively studied in various areas including biological chemistry, inhibition studies, supramolecular chemistry, and protein arrays.
Synthetic chemical probes are powerful tools for investigating biological processes. They are particularly useful for proteomic studies such as activity-based protein profiling (ABPP). These chemical methods initially used mimics of natural substrates. As the techniques gained prominence, more and more elaborate chemical probes with increased specificity towards given enzyme/protein families and amenability to various reaction conditions were used. Among the chemical probes, peptidyl-epoxysuccinates represent one of the first types of compounds used to investigate the activity of the cysteine protease papain-like family of enzymes. Structurally derived from the natural substrate, a wide body of inhibitors and activity- or affinity-based probes bearing the electrophilic oxirane unit for covalent labeling of active enzymes now exists. Herein, we review the literature regarding the synthetic approaches to epoxysuccinate-based chemical probes together with their reported applications, from biological chemistry and inhibition studies to supramolecular chemistry and the formation of protein arrays.
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