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10.1016/j.bbapap.2020.140445

http://scihub22266oqcxt.onion/10.1016/j.bbapap.2020.140445
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32405284!7219385!32405284
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suck abstract from ncbi


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pmid32405284      Biochim+Biophys+Acta+Proteins+Proteom 2020 ; 1868 (9): 140445
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  • Coumarin as a structural component of substrates and probes for serine and cysteine proteases #MMPMID32405284
  • Breidenbach J; Bartz U; Gutschow M
  • Biochim Biophys Acta Proteins Proteom 2020[Sep]; 1868 (9): 140445 PMID32405284show ga
  • Coumarins represent well-established structures to introduce fluorescence into tool compounds for biochemical investigations. They are valued for their small size, chemical stability and accessibility as well as their tunable photochemical properties. As components of fluorophore/quencher pairs or FRET donor/acceptor pairs, coumarins have frequently been applied in substrate mapping approaches for serine and cysteine proteases. This review also focuses on the incorporation of coumarins into the side chain of amino acids and the exploitation of the resulting fluorescent amino acids for the positional profiling of protease substrates. The protease-inhibiting properties of certain coumarin derivatives and the utilization of coumarin moieties to assemble activity-based probes for serine and cysteine proteases are discussed as well.
  • |Catalytic Domain[MESH]
  • |Coumarins/*chemistry/*metabolism/pharmacology[MESH]
  • |Cysteine Proteases/drug effects/*metabolism[MESH]
  • |Fluorescence[MESH]
  • |Fluorescence Resonance Energy Transfer/methods[MESH]
  • |Fluorescent Dyes/chemistry[MESH]
  • |Serine Proteases/drug effects/*metabolism[MESH]
  • |Serine/metabolism[MESH]


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