2. Academic Validation
  3. Broad spectrum antiprotozoal agents that inhibit histone deacetylase: structure-activity relationships of apicidin. Part 2

Broad spectrum antiprotozoal agents that inhibit histone deacetylase: structure-activity relationships of apicidin. Part 2

  • Bioorg Med Chem Lett. 2001 Jan 22;11(2):113-7. doi: 10.1016/s0960-894x(00)00605-3.
S L Colletti 1,  R W Myers,  S J Darkin-Rattray,  A M Gurnett,  P M Dulski,  S Galuska,  J J Allocco,  M B Ayer,  C Li,  J Lim,  T M Crumley,  C Cannova,  D M Schmatz,  M J Wyvratt,  M H Fisher,  P T Meinke
Affiliations

Affiliation

  • 1 Merck Research Laboratories, Merck & Co., Inc., Rahway, NJ 07065, USA. steve_colletti@merck.com
PMID: 11206439 DOI: 10.1016/s0960-894x(00)00605-3
Abstract

Recently isolated at Merck, apicidin inhibits both mammalian and protozoan histone deacetylases (HDACs). The conversion of apicidin, a nonselective nanomolar inhibitor of HDACs, into a series of picomolar indole-modified and parasite-selective tryptophan-replacement analogues is described within this structure-activity study.

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