Constraining the amide bond in N-sulfonylated dipeptide VLA-4 antagonists

Bioorg Med Chem Lett. 2008 Mar 1;18(5):1688-91. doi: 10.1016/j.bmcl.2008.01.045. Epub 2008 Jan 18.

Abstract

The integrin VLA-4 is implicated in several inflammatory disease states. In search of non-peptidic antagonists of VLA-4, rotational constraints were imposed on the amide bond of prototypical N-sulfonylated dipeptide VLA-4 antagonists. By judicious structural modification of the side chains, trisubstituted imidazoles with moderate binding potencies were obtained, for example, 19, VLA-4 IC(50)=237 nM.

MeSH terms

  • Dipeptides / chemistry*
  • Dipeptides / pharmacology*
  • Integrin alpha4beta1 / antagonists & inhibitors*
  • Molecular Structure
  • Receptors, Very Late Antigen / chemistry
  • Structure-Activity Relationship

Substances

  • Dipeptides
  • Integrin alpha4beta1
  • Receptors, Very Late Antigen