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.
S B Singh  1 ,  D L Zink ,  J M Liesch ,  A W Dombrowski ,  S J Darkin-Rattray ,  D M Schmatz ,  M A Goetz
Affiliations
  • 1. Merck Research Laboratories, RY80Y-355, P.O. Box 2000, Rahway, New Jersey 07065, USA. [email protected]
PMID: 11529764 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.

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