Design, synthesis and biological evaluation of carboxy analogues of arginine methyltransferase inhibitor 1 (AMI-1)

ChemMedChem. 2010 Mar 1;5(3):398-414. doi: 10.1002/cmdc.200900459.

Abstract

Here we report the synthesis of a number of compounds structurally related to arginine methyltransferase inhibitor 1 (AMI-1). The structural alterations that we made included: 1) the substitution of the sulfonic groups with the bioisosteric carboxylic groups; 2) the replacement of the ureidic function with a bis-amidic moiety; 3) the introduction of a N-containing basic moiety; and 4) the positional isomerization of the aminohydroxynaphthoic moiety. We have assessed the biological activity of these compounds against a panel of arginine methyltransferases (fungal RmtA, hPRMT1, hCARM1, hPRMT3, hPRMT6) and a lysine methyltransferase (SET7/9) using histone and nonhistone proteins as substrates. Molecular modeling studies for a deep binding-mode analysis of test compounds were also performed. The bis-carboxylic acid derivatives 1 b and 7 b emerged as the most effective PRMT inhibitors, both in vitro and in vivo, being comparable or even better than the reference compound (AMI-1) and practically inactive against the lysine methyltransferase SET7/9.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Aspergillus nidulans / enzymology
  • Binding Sites
  • Fungal Proteins / antagonists & inhibitors
  • Fungal Proteins / chemistry
  • Fungal Proteins / metabolism
  • Histone-Lysine N-Methyltransferase / antagonists & inhibitors
  • Histone-Lysine N-Methyltransferase / metabolism
  • Humans
  • Intracellular Signaling Peptides and Proteins
  • Methyltransferases / antagonists & inhibitors*
  • Methyltransferases / chemistry
  • Methyltransferases / metabolism*
  • Models, Molecular
  • Naphthalenesulfonates / chemistry*
  • Naphthalenesulfonates / pharmacology*
  • Protein Conformation
  • Protein-Arginine N-Methyltransferases
  • Quantitative Structure-Activity Relationship
  • Urea / analogs & derivatives*
  • Urea / chemistry
  • Urea / pharmacology

Substances

  • 7,7'-carbonylbis(azanediyl) bis(4-hydroxynaphthalene-2-sulfonic acid
  • Fungal Proteins
  • Intracellular Signaling Peptides and Proteins
  • Naphthalenesulfonates
  • Urea
  • Methyltransferases
  • PRMT2 protein, human
  • Protein-Arginine N-Methyltransferases
  • Histone-Lysine N-Methyltransferase