Structure-based design of carboxybiphenylindole inhibitors of the ZipA-FtsZ interaction

Org Biomol Chem. 2003 Dec 7;1(23):4138-40. doi: 10.1039/b312016c. Epub 2003 Oct 29.

Abstract

Structural features of two weak inhibitors of the ZipA-FtsZ protein-protein interaction which were found to bind to overlapping but different areas of the key binding site were combined in one new series of carboxybiphenyl-indoles with improved inhibitory activity.

MeSH terms

  • Bacterial Proteins / antagonists & inhibitors
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / metabolism*
  • Carrier Proteins / antagonists & inhibitors
  • Carrier Proteins / chemistry
  • Carrier Proteins / metabolism*
  • Cell Cycle Proteins / antagonists & inhibitors
  • Cell Cycle Proteins / chemistry
  • Cell Cycle Proteins / metabolism*
  • Cytoskeletal Proteins / antagonists & inhibitors
  • Cytoskeletal Proteins / chemistry
  • Cytoskeletal Proteins / metabolism*
  • Drug Design*
  • Escherichia coli Proteins / antagonists & inhibitors
  • Escherichia coli Proteins / chemistry
  • Escherichia coli Proteins / metabolism*
  • Indoles / chemistry*
  • Indoles / pharmacology*
  • Inhibitory Concentration 50
  • Models, Molecular
  • Molecular Structure
  • Protein Binding / drug effects
  • Protein Structure, Tertiary
  • Structure-Activity Relationship

Substances

  • Bacterial Proteins
  • Carrier Proteins
  • Cell Cycle Proteins
  • Cytoskeletal Proteins
  • Escherichia coli Proteins
  • FtsZ protein, Bacteria
  • Indoles
  • ZipA protein, E coli
  • indole