Structure, histone deacetylase, and antiprotozoal activities of apicidins B and C, congeners of apicidin with proline and valine substitutions.
[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.
Singh
S B
SB
Merck Research Laboratories, RY80Y-355, P.O. Box 2000, Rahway, New Jersey 07065, USA. sheo_singh@merck.com
Zink
D L
DL
Liesch
J M
JM
Dombrowski
A W
AW
Darkin-Rattray
S J
SJ
Schmatz
D M
DM
Goetz
M A
MA
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
D000981:Antiprotozoal Agents; D056572:Histone Deacetylase Inhibitors; D010456:Peptides, Cyclic; C102351:apicidin; D011392:Proline; D006655:Histone Deacetylases; D014633:Valine