2. Academic Validation
  3. Structure, histone deacetylase, and antiprotozoal activities of apicidins B and C, congeners of apicidin with proline and valine substitutions

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

Affiliation

  • 1 Merck Research Laboratories, RY80Y-355, P.O. Box 2000, Rahway, New Jersey 07065, USA. sheo_singh@merck.com
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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