Smallpox Antiviral Drug

Abstract

Using a homology-based bioinformatics approach, a structural model of the vaccinia virus (VV) I7L proteinase was developed at Transtech Pharma. A unique chemical library of ~ 51,000 compounds was computationally queried to identify potential active site inhibitors. The resulting biased subset of compounds was assayed for both toxicity and the ability to inhibit the growth of VV in tissue culture cells and found to target the I7L enzyme. However, after several rounds of medicinal chemistry the chemists were not able to improve the pharmacokinetic and toxicological properties of this series of compounds. SIGA has since designed a new structural model of the I7L active site based on the Ulp1 cysteine proteinase (PDB: 1euv). Commercially available small molecule libraries that total approximately 1 million compounds are currently being queried to identify potential inhibitors. Potential active site inhibitors are being purchased and tested in the recently developed in vitro I7L cleavage assay. A new fluorescence anisotrophy cleavage assay is under development and will be converted to a high-throughput screen if possible. SIGA has a 200,000 small molecule library that could be used for screening in a HTS cleavage assay. The final goal of this project is the identification of a potent antiviral against various pox viruses ready for preclinical development.

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Document Details

Document Type
Technical Report
Publication Date
Jan 01, 2006
Accession Number
ADA462351

Entities

People

  • Dennis E. Hruby

Tags

DTIC Thesaurus Topics

  • Biochemistry
  • Cells
  • Chemical Synthesis
  • Chemistry
  • Cysteine
  • Dna Viruses
  • Enzyme Inhibitors
  • Identification
  • Inhibitors
  • Lepidoptera
  • Molecules
  • Poxviridae Infections
  • Proteins
  • Small Molecules
  • Tissue Culture
  • Virology
  • Viruses

Fields of Study

  • Chemistry

Readers

  • Computational Modeling and Simulation
  • Molecular and Cellular Biochemistry
  • Oncology