Structure, histone deacetylase, and antiprotozoal activities of apicidins B and C, congeners of apicidin with proline and valine substitutions

Authors
Singh, SB Zink, DL Liesch, JM Dombrowski, AW Darkin-Rattray, SJ Schmatz, DM Goetz, MA
Citation
Sb. Singh et al., Structure, histone deacetylase, and antiprotozoal activities of apicidins B and C, congeners of apicidin with proline and valine substitutions, ORG LETT, 3(18), 2001, pp. 2815-2818
Citations number
22
Categorie Soggetti
Organic Chemistry/Polymer Science
Journal title
ORGANIC LETTERS
ISSN journal
15237060 → ACNP
Volume
3
Issue
18
Year of publication
2001
Pages
2815 - 2818
Database
ISI
SICI code
1523-7060(20010906)3:18<2815:SHDAAA>2.0.ZU;2-N
Abstract
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 cy clic 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.