title: Structure, histone deacetylase, and antiprotozoal activities of apicidins B and C, congeners of apicidin with proline and valine substitutions.
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.
authors.affiliation: Merck Research Laboratories, RY80Y-355, P.O. Box 2000, Rahway, New Jersey 07065, USA. sheo_singh@merck.com
authors.forename: S B
authors.initials: SB
authors.lastname: Singh
authors.forename: D L
authors.initials: DL
authors.lastname: Zink
authors.forename: J M
authors.initials: JM
authors.lastname: Liesch
authors.forename: A W
authors.initials: AW
authors.lastname: Dombrowski
authors.forename: S J
authors.initials: SJ
authors.lastname: Darkin-Rattray
authors.forename: D M
authors.initials: DM
authors.lastname: Schmatz
authors.forename: M A
authors.initials: MA
authors.lastname: Goetz
mesh_terms: D019943:Amino Acid Substitution; D000818:Animals; D000981:Antiprotozoal Agents / Q000737:chemistry* / Q000494:pharmacology; D016786:Eimeria tenella / Q000187:drug effects; D056572:Histone Deacetylase Inhibitors; D006655:Histone Deacetylases / Q000378:metabolism*; D009682:Magnetic Resonance Spectroscopy; D008968:Molecular Conformation; D021261:Parasitic Sensitivity Tests; D010456:Peptides, Cyclic / Q000737:chemistry* / Q000494:pharmacology; D011392:Proline / Q000737:chemistry; D021745:Sarcocystidae / Q000187:drug effects; D014633:Valine / Q000737:chemistry
chemical_list: D000981:Antiprotozoal Agents; D056572:Histone Deacetylase Inhibitors; D010456:Peptides, Cyclic; C102351:apicidin; D011392:Proline; D006655:Histone Deacetylases; D014633:Valine