Caspase Inhibitors

Caspase inhibitors are designed by combination of caspase specific peptide sequences with functional groups. Due to the lower reactivity of the aldehyde (CHO) function, these caspase inhibitors act usually reversible whereas caspase inhibitors with chloromethylketone (CMK) and fluoromethylketone (FMK) react irreversible with the related enzyme. The specificity of the caspase inhibitor according to the target is determined by the enzyme recognition sequence. For example, the tripeptide Z-VAD-FMK is used as broad-range irreversible caspase inhibitor whereas the tetrapeptides Ac-YVAD-CHO and Ac-WEHD-CHO shows stronger, but reversible selectivity to Caspase-1. All caspase inhibitors offered from PeptaNova are synthetic products manufactured by Peptide Institute under highest quality standards.

Links to publications that used our caspase specific inhibitors:

  1. Characterization of ochratoxin A-induced apoptosis in primary rat hepatocytes
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