Inhibitors of the hepatitis C virus NS3 protease with basic amine functionality at the P3-amino acid N-terminus: discovery and optimization of a new series of P2-P4 macrocycles

J Med Chem. 2009 Aug 13;52(15):4820-37. doi: 10.1021/jm900372w.

Abstract

In a follow-up to our recent disclosure of P2-P4 macrocyclic inhibitors of the hepatitis C virus (HCV) NS3 protease (e.g., 1, Chart 1), we report a new but related compound series featuring a basic amine at the N-terminus of the P3-amino acid residue. Replacement of the electroneutral P3-amino acid capping group (which is a feature of almost all tripeptide-like inhibitors of NS3 reported to date) with a basic group is not only tolerated but can result in advantageous cell based potency. Optimization of this new class of P3-amine based inhibitors gave compounds such as 25 and 26 that combine excellent cell based activity with pharmacokinetic properties that are attractive for an antiviral targeting HCV.

MeSH terms

  • Amines / chemical synthesis*
  • Amines / pharmacokinetics
  • Amines / pharmacology
  • Animals
  • Antiviral Agents / chemical synthesis*
  • Antiviral Agents / pharmacokinetics
  • Antiviral Agents / pharmacology
  • Dogs
  • Drug Discovery
  • Male
  • Rats
  • Rats, Sprague-Dawley
  • Structure-Activity Relationship
  • Viral Nonstructural Proteins / antagonists & inhibitors*

Substances

  • Amines
  • Antiviral Agents
  • NS3 protein, hepatitis C virus
  • Viral Nonstructural Proteins