Hydrophobic benzoic acids as inhibitors of influenza neuraminidase

Bioorg Med Chem. 1999 Nov;7(11):2487-97. doi: 10.1016/s0968-0896(99)00197-2.

Abstract

Neuraminidase (NA) plays a critical role in the life cycle of influenza virus and is a target for new therapeutic agents. A new benzoic acid inhibitor (11) containing a lipophilic side chain at C-3 and a guanidine at C-5 was synthesized. The X-ray structure of 4-(N-acetylamino)-5-guanidino-3-(3-pentyloxy)benzoic acid in complex with NA revealed that the lipophilic side chain binds in a newly created hydrophobic pocket formed by the movement of Glu 278 to interact with Arg 226, whereas the guanidine of 11 interacts in a negatively charged pocket created by Asp 152, Glu 120 and Glu 229. Compound 11 was highly selective for type A (H2N2) influenza NA (IC50 1 microM) over type B (B/Lee/40) influenza NA (IC50 500 microM).

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Antiviral Agents / chemical synthesis
  • Antiviral Agents / pharmacology
  • Benzoates / chemical synthesis
  • Benzoates / chemistry
  • Benzoates / pharmacology*
  • Crystallography, X-Ray
  • Enzyme Inhibitors / chemical synthesis
  • Enzyme Inhibitors / pharmacology
  • Models, Molecular
  • Neuraminidase / antagonists & inhibitors*
  • Neuraminidase / chemistry
  • Orthomyxoviridae / drug effects*
  • Orthomyxoviridae / enzymology
  • Protein Conformation

Substances

  • Antiviral Agents
  • Benzoates
  • Enzyme Inhibitors
  • Neuraminidase