Design and synthesis of aminophenol-based factor Xa inhibitors

Bioorg Med Chem Lett. 2002 May 6;12(9):1307-10. doi: 10.1016/s0960-894x(02)00142-7.

Abstract

A novel potent and selective aminophenol scaffold for fXa inhibitors was developed from a previously reported benzimidazole-based naphthylamidine template. The aminophenol template is more synthetically accessible than the benzimidazole template, which simplified the introduction of carboxylic acid groups. Substitution of a propenyl-para-hydroxy-benzamidine group on the aminophenol template produced selective, sub-nanomolar fXa inhibitors. The potency of the inhibitors is partially explained with the aid of a trypsin complex crystal structure.

MeSH terms

  • Aminophenols / chemical synthesis*
  • Aminophenols / chemistry*
  • Factor Xa Inhibitors*
  • Serine Proteinase Inhibitors / chemical synthesis*
  • Serine Proteinase Inhibitors / chemistry*
  • X-Ray Diffraction

Substances

  • Aminophenols
  • Factor Xa Inhibitors
  • Serine Proteinase Inhibitors