Comparison of inhibitory activity of isomeric triazolopyridine derivatives towards adenosine receptor subtypes or do similar structures reveal similar bioactivities?

Bioorg Med Chem Lett. 2004 Jun 21;14(12):3307-12. doi: 10.1016/j.bmcl.2004.03.104.

Abstract

The synthesis of an array of 8-amino-2-aryl-[1,2,4]triazolo[1,5-a]pyridine-6-carboxyl amide derivatives is described for the first time. A subset of 20 derivatives were compared to their isomeric 5-amino-2-aryl-[1,2,4]triazolo[1,5-a]pyridine-7-carboxyl amide counterparts with regard to their potential to inhibit the human adenosine 2a (hA2a) receptor and their selectivity against the human adenosine 1 (hA1) receptor. Based on the analysis of H-bond donor/acceptor capabilities of the isomeric triazolopyridine pairs it can be concluded that the H-bond donor strength of the free amino functionality is the main determinant for hA2a inhibitory activity and hA1 selectivity.

Publication types

  • Comparative Study

MeSH terms

  • Binding Sites
  • Humans
  • Purinergic P1 Receptor Antagonists*
  • Pyridines / chemistry*
  • Pyridines / metabolism
  • Pyridines / pharmacology
  • Receptors, Purinergic P1 / metabolism
  • Structure-Activity Relationship
  • Triazoles / chemistry*
  • Triazoles / metabolism
  • Triazoles / pharmacology

Substances

  • Purinergic P1 Receptor Antagonists
  • Pyridines
  • Receptors, Purinergic P1
  • Triazoles