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Highly functionalized terpyridines as competitive inhibitors of AKAP-PKA interactions

Authors

  • G. Schäfer
  • J Milić
  • A Eldahshan
  • F. Götz
  • K. Zühlke
  • C. Schillinger
  • A. Kreuchwig
  • J.M. Elkins
  • K.R.A. Abdul Azeez
  • A. Oder
  • M.C. Moutty
  • N. Masada
  • M. Beerbaum
  • B. Schlegel
  • S. Niquet
  • P. Schmieder
  • G. Krause
  • J.P. von Kries
  • D.M.F. Cooper
  • S. Knapp
  • J. Rademann
  • W. Rosenthal
  • E. Klussmann

Journal

  • Angewandte Chemie International Edition

Citation

  • Angew Chem Int Ed 52 (46): 12187-12191

Abstract

  • A good fit: Interactions between A-kinase anchoring proteins (AKAPs) and protein kinase A (PKA) play key roles in a plethora of physiologically relevant processes whose dysregulation causes or is associated with diseases such as heart failure. Terpyridines have been developed as α-helix mimetics for the inhibition of such interactions and are the first biologically active, nonpeptidic compounds that block the AKAP binding site of PKA.


DOI

doi:10.1002/anie.201304686