Fluoro-Olefins as Peptidomimetic Inhibitors of Dipeptidyl Peptidases
Journal of Medicinal Chemistry2004Vol. 48(6), pp. 1768–1780
Citations Over TimeTop 11% of 2004 papers
Pieter Van der Veken, Kristel Senten, István Kertész, Ingrid De Meester, Anne‐Marie Lambeir, Marie-Berthe Maes, Simon Scharpé, Achiel Haemers, Koen Augustyns
Abstract
The feasibility of the fluoro-olefin function as a peptidomimetic group in inhibitors for dipeptidyl peptidase IV and II (DPP IV and DPP II) is investigated by evaluation of N-substituted Gly-Psi[CF=C]pyrrolidines, Gly-Psi[CF=C]piperidines, and Gly-Psi[CF=C](2-cyano)pyrrolidines. Of this later class, the (Z)- and (E)-fluoro-olefin analogues were prepared and chemical stability in comparison with the parent amide was checked. Most of these compounds exhibited a strong binding preference toward DPP II with IC(50) values in the low micromolar range, while only low DPP IV inhibitory potential is seen.
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