Abstract
Phosphorus-containing inhibitors, such as diisopropyl phosphorofluoride (DFP), are classical inhibitors of serine proteases. These compounds react irreversibly with the active site serine hydroxy group, forming a covalent adduct. Nonpeptidyl phosphorylating agents do not discriminate between various serine proteases due to their lack of structural similarity with natural peptide substrates. Substrate-related peptidyl α-aminophosphonic acids have great potential for producing selective serine protease inhibitors1–4 since they form stable transition-state analogues with the active site serine residue, similar to the tetrahedral intermediates formed during normal substrate hydrolysis.
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