Multitarget, Selective Compound Design Yields Potent Inhibitors of a Kinetoplastid Pteridine Reductase 1

J Med Chem. 2022 Jul 14;65(13):9011-9033. doi: 10.1021/acs.jmedchem.2c00232. Epub 2022 Jun 8.

Abstract

The optimization of compounds with multiple targets is a difficult multidimensional problem in the drug discovery cycle. Here, we present a systematic, multidisciplinary approach to the development of selective antiparasitic compounds. Computational fragment-based design of novel pteridine derivatives along with iterations of crystallographic structure determination allowed for the derivation of a structure-activity relationship for multitarget inhibition. The approach yielded compounds showing apparent picomolar inhibition of T. brucei pteridine reductase 1 (PTR1), nanomolar inhibition of L. major PTR1, and selective submicromolar inhibition of parasite dihydrofolate reductase (DHFR) versus human DHFR. Moreover, by combining design for polypharmacology with a property-based on-parasite optimization, we found three compounds that exhibited micromolar EC50 values against T. brucei brucei while retaining their target inhibition. Our results provide a basis for the further development of pteridine-based compounds, and we expect our multitarget approach to be generally applicable to the design and optimization of anti-infective agents.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Leishmania major* / drug effects
  • Leishmania major* / enzymology
  • Oxidoreductases* / antagonists & inhibitors
  • Oxidoreductases* / metabolism
  • Pteridines / chemistry
  • Pteridines / pharmacology
  • Structure-Activity Relationship
  • Tetrahydrofolate Dehydrogenase* / metabolism
  • Trypanosoma brucei brucei* / drug effects
  • Trypanosoma brucei brucei* / enzymology

Substances

  • Pteridines
  • Oxidoreductases
  • pteridine reductase
  • Tetrahydrofolate Dehydrogenase