Synthesis of 2-amino-3-heteroaroylthiophenes and evaluation of their activity as potential allosteric enhancers at the human A1 receptor

Eur J Med Chem. 2004 Oct;39(10):855-65. doi: 10.1016/j.ejmech.2004.06.009.

Abstract

2-Amino-3-benzoylthiophenes are allosteric enhancers of agonist binding to the adenosine A(1) receptor. New compounds bearing an heteroaroyl instead of the benzoyl moiety at the 3-position of the thiophene were synthesized. The phenyl ring was replaced with heterocycles that possess heteroatoms able to form hydrogen bonds (2-furanyl, 2-benzofuranyl, 2-pyridinyl in compounds 2-13) or with a thienyl moiety as isoster of the phenyl ring (2-thienyl, 3-thienyl and 5-halo-2-thienyl in compounds 14-29). The effect of several alkyl substituents at positions 4 and 5 of the thiophene ring to increase enhancer activity was determined. The ability of the new molecules to reduce the cAMP content in CHO cells expressing the human adenosine A(1) receptor was evaluated. Compounds 2-13 with hydrogen bond-forming heteroatoms did not show significant activity as allosteric enhancers. On the other hand, compounds 15-16 and 19-20 with an unsubstituted thienyl moiety as replacement for the phenyl ring were nearly as efficacious as PD 81,723, the prototypical A(1) allosteric enhancer. Alkyl substituents at positions 4 and 5 of the thiophene ring were tolerated while a substituted piperidine ring was not tolerated. We conclude that hydrogen bonds could not be formed in the domain of the receptor that accommodates the phenyl ring of 2-amino-3-benzoylthiophene derivatives, indicating that this domain is hydrophobic.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Allosteric Regulation / drug effects
  • Allosteric Regulation / physiology
  • Animals
  • Cerebral Cortex / drug effects
  • Cerebral Cortex / metabolism
  • Cricetinae
  • Drug Evaluation, Preclinical / methods
  • Humans
  • Male
  • Protein Binding / drug effects
  • Protein Binding / physiology
  • Rats
  • Rats, Wistar
  • Receptor, Adenosine A1 / metabolism*
  • Thiophenes / chemical synthesis*
  • Thiophenes / metabolism*
  • Thiophenes / pharmacology

Substances

  • Receptor, Adenosine A1
  • Thiophenes