Inhibition of recombinant dipeptidyl peptidase III by synthetic hemorphin-like peptides
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Updated: Sep 20, 2026

Peptide-based Identification of Functional Motifs and their Binding Partners
Published on: June 30, 2013
Takehiro Chiba1, Yao-Hua Li, Takuya Yamane
1Department of Orthopaedics, Nagoya City University Medical School, Mizuho-ku, 467-8601 Nagoya, Japan.
Abstract:
In order to find the most effective antagonist for dipeptidyl peptidase III degrading enkephalin, we synthesized hemorphin-like pentapeptides with aliphatic or aromatic amino acids at the N-termini, such as VVYPW, LVYPW, IVYPW, YVYPW, FVYPW and WVYPW. Among those pentapeptides, IVYPW and WVYPW showed the strongest inhibitory activity toward rDPP III. The K(i) values of IVYPW and WVYPW were 0.100+/-0.011 and 0.126+/-0.015 microM (mean+/-S.E.), respectively. The order of K(i) values was Ile> or =Trp>Phe> or =Tyr>Leu>Ala>Val>Ser>Gly. rDPP III activity is inhibited in a non-competitive manner by these peptides. The peptide VYPW did not inhibit rDPP III activity, but the sequence is essential for the expression of inhibitory activity.
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