Bioorganic and Medicinal Chemistry Letters p. 1237 - 1240 (1996)
Update date:2022-08-04
Topics:
Chatterjee, Sankar
Josef, Kurt
Wells, Gregory
Iqbal, Mohamed
Bihovsky, Ron
Mallamo, John P.
Ator, Mark A.
Bozyczko-Coyne, Donna
Mallya, Satish
Senadhi, Shobha
Siman, Robert
We report on a series of potent and selective dipeptide fluoromethyl ketone inhibitors of recombinant human calpain I. Compound 4f, having a tetrahydroisoquinoline containing urea motif as N-terminus capping group, is the most potent member (k(obs)/I = 276,000 M-1 s-1) of this class. This compound was shown to prefer calpain I by >36-fold and approximately 4-fold over the related cysteine proteases, cathepsin B and cathepsin L, respectively.
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