Synthesis and structure-activity relationships of potent 3- or 4-substituted-2-cyanopyrrolidine dipeptidyl peptidase IV inhibitors

Bioorg Med Chem. 2004 Dec 1;12(23):6053-61. doi: 10.1016/j.bmc.2004.09.010.

Abstract

Dipeptidyl peptidase IV (DPP-IV) inhibitors have attracted attention as potential drugs for use in the treatment of type 2 diabetes because they prevent degradation of glucagon-like peptide-1 (GLP-1) and extend its duration of action. A series of 2-cyanopyrrolidines are among the most potent of DPP-IV inhibitors. We focused our attention on substitutions at the 3- or 4-position of 2-cyanopyrrolidines and synthesized and evaluated various derivatives. Among them, the 4-fluoro derivative was found to exhibit better DPP-IV inhibitory activity and higher plasma drug concentrations after oral administration to rats than the 4-unsubstituted derivative. We report here on the synthesis and biological data of the aforementioned derivatives.

MeSH terms

  • Adenosine Deaminase Inhibitors*
  • Administration, Oral
  • Animals
  • Blood Glucose / drug effects
  • Dipeptidyl Peptidase 4
  • Enzyme Inhibitors / blood
  • Enzyme Inhibitors / chemical synthesis
  • Enzyme Inhibitors / pharmacology
  • Glycoproteins / antagonists & inhibitors*
  • Humans
  • Inhibitory Concentration 50
  • Molecular Structure
  • Pharmacokinetics
  • Pyrrolidines / blood
  • Pyrrolidines / chemical synthesis*
  • Pyrrolidines / pharmacology
  • Rats
  • Rats, Wistar
  • Structure-Activity Relationship

Substances

  • Adenosine Deaminase Inhibitors
  • Blood Glucose
  • Enzyme Inhibitors
  • Glycoproteins
  • Pyrrolidines
  • DPP4 protein, human
  • Dipeptidyl Peptidase 4