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- W2063532783 abstract "Peptidyl α-aminoalkylphosphonate diphenyl esters have been synthesized and shown to be effective inhibitors of serine proteases. Extending the peptide chain from a single α-aminoalkylphosphonate residue (kobs[I]=2.5−260 M−1s−1) to a tripeptide or tetrapeptide derivative (kobs[I]=7,000−17,000 M−1s−1) resulted in 65–2800 improvement in inhibitory potency and increased specificity. The rate of inactivation of chymotrypsin by MeO-Suc-Ala-Ala-Pro-HNCH (CH2Ph) P (O) (OPh)2 was decreased 5 fold in the presence of the substrate Suc-Val-Pro-Phe-NA (0.119 mM). Phosphonylated serine proteases are extremely stable since the half-life for reactivation was >48 hrs for the inhibited elastases and at least 10 hrs for chymotrypsin." @default.
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- W2063532783 date "1989-05-01" @default.
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- W2063532783 title "Irreversible inhibition of serine proteases by peptidyl derivatives of α-aminoalkylphosphonate diphenyl esters" @default.
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- W2063532783 doi "https://doi.org/10.1016/0006-291x(89)91572-6" @default.
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