Design, synthesis, and biological evaluation of O-2-modified indenoisoquinolines as dual topoisomerase I-tyrosyl-DNA phosphodiesterase I inhibitors

J Med Chem. 2014 May 22;57(10):4324-36. doi: 10.1021/jm500294a. Epub 2014 May 6.

Abstract

Tyrosyl-DNA phosphodiesterase I (TDP1) repairs stalled topoisomerase I (Top1)-DNA covalent complexes and has been proposed to be a promising and attractive target for cancer treatment. Inhibitors of TDP1 could conceivably act synergistically with Top1 inhibitors and thereby potentiate the effects of Top1 poisons. This study describes the successful design and synthesis of 2-position-modified indenoisoquinolines as dual Top1-TDP1 inhibitors using a structure-based drug design approach. Enzyme inhibition studies indicate that indenoisoquinolines modified at the 2-position with three-carbon side chains ending with amino substituents show both promising Top1 and TDP1 inhibitory activity. Molecular modeling of selected target compounds bound to Top1 and TDP1 was used to rationalize the enzyme inhibition results and structure-activity relationship analysis.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, N.I.H., Intramural
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Drug Design
  • Humans
  • Isoquinolines / chemical synthesis*
  • Isoquinolines / pharmacology
  • Models, Molecular
  • Phosphodiesterase Inhibitors / chemical synthesis*
  • Phosphodiesterase Inhibitors / chemistry
  • Phosphodiesterase Inhibitors / pharmacology
  • Phosphoric Diester Hydrolases / chemistry
  • Phosphoric Diester Hydrolases / drug effects*
  • Structure-Activity Relationship
  • Topoisomerase I Inhibitors / chemical synthesis*
  • Topoisomerase I Inhibitors / chemistry
  • Topoisomerase I Inhibitors / pharmacology

Substances

  • Isoquinolines
  • Phosphodiesterase Inhibitors
  • Topoisomerase I Inhibitors
  • Phosphoric Diester Hydrolases
  • TDP1 protein, human