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Structure, histone deacetylase, and antiprotozoal activities of apicidins B and C, congeners of apicidin with proline and valine substitutions.
- Source :
-
Organic letters [Org Lett] 2001 Sep 06; Vol. 3 (18), pp. 2815-8. - Publication Year :
- 2001
-
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.
- Subjects :
- Amino Acid Substitution
Animals
Antiprotozoal Agents pharmacology
Eimeria tenella drug effects
Histone Deacetylase Inhibitors
Magnetic Resonance Spectroscopy
Molecular Conformation
Parasitic Sensitivity Tests
Peptides, Cyclic pharmacology
Proline chemistry
Sarcocystidae drug effects
Valine chemistry
Antiprotozoal Agents chemistry
Histone Deacetylases metabolism
Peptides, Cyclic chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 1523-7060
- Volume :
- 3
- Issue :
- 18
- Database :
- MEDLINE
- Journal :
- Organic letters
- Publication Type :
- Academic Journal
- Accession number :
- 11529764
- Full Text :
- https://doi.org/10.1021/ol016240g