Structure, histone deacetylase, and antiprotozoal activities of apicidins B and C, congeners of apicidin with proline and valine substitutions

Org Lett. 2001 Sep 6;3(18):2815-8. doi: 10.1021/ol016240g.

Abstract

[structure: see text]. Isolation and structure elucidation of two novel cyclic tetrapeptides that show a variety of potent antiprotozoal activities by reversibly inhibiting HDAC have been reported. These are the new members of a unique family of cyclic tetrapeptides that do not require the electrophilic alpha-epoxyketone moiety of HC-toxin, trapoxin A, or chlamydocin for their potent activities against HDAC and the malarial parasite.

MeSH terms

  • Amino Acid Substitution
  • Animals
  • Antiprotozoal Agents / chemistry*
  • Antiprotozoal Agents / pharmacology
  • Eimeria tenella / drug effects
  • Histone Deacetylase Inhibitors
  • Histone Deacetylases / metabolism*
  • Magnetic Resonance Spectroscopy
  • Molecular Conformation
  • Parasitic Sensitivity Tests
  • Peptides, Cyclic / chemistry*
  • Peptides, Cyclic / pharmacology
  • Proline / chemistry
  • Sarcocystidae / drug effects
  • Valine / chemistry

Substances

  • Antiprotozoal Agents
  • Histone Deacetylase Inhibitors
  • Peptides, Cyclic
  • apicidin
  • Proline
  • Histone Deacetylases
  • Valine