Open AccessInhibition of Dipeptidyl Peptidase iv (CD26) by Peptide Boronic Acid Dipeptides
Author(s) -
Pargellis Ca,
Campbell Sj,
Pav S,
Graham Et,
Pitner Tp
Publication year - 1997
Publication title -
journal of enzyme inhibition
Language(s) - English
Resource type - Journals
eISSN - 1029-2462
pISSN - 1026-5457
DOI - 10.3109/14756369709027647
Subject(s) - dipeptidyl peptidase , peptide , chemistry , boronic acid , biochemistry , enzyme , dipeptidyl peptidase 4 , amino acid , stereochemistry , combinatorial chemistry , biology , endocrinology , diabetes mellitus , type 2 diabetes
Peptide boronic acid dipeptide compounds were analyzed for their ability to inhibit recombinant human dipeptidylpeptidase IV (CD26, DPPIV). Rate constants for the peptide boronates are difficult to obtain because the active boronic acid dipeptide exists in equilibrium with a cyclic inactive species in aqueous solution. Rate constants were determined for the inhibition of DPPIV using several peptide boronates at different pH values. Val-boroPro forms the most tightly bound complex with DPPIV; the first order half life for dissociation of the inactive enzyme-inhibitor complex at 23 degrees C is approximately 27 days.