Abstract
A member of the cyclic hexadepsipeptide family, PD124,966, isolated from a fermentation product of an actinomycete, inhibited poly(ADP-ribose) glycohydrolase (Parg) with IC50 of 40 μg/ml. A novel cyclic peptide, pargamicin, isolated from a fermentation broth of Amicolatopsis sp., also inhibited Parg with IC50 of 28 μg/ml. A linear peptide containing piperazic acid residues, piperastatin A, isolated from Streptomyces lavendofoliae, did not inhibit Parg activity.
Original language | English |
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Pages (from-to) | 15-17 |
Number of pages | 3 |
Journal | Proceedings of the Japan Academy Series B: Physical and Biological Sciences |
Volume | 78 |
Issue number | 1 |
DOIs | |
Publication status | Published - 2002 Jan |
Externally published | Yes |
Keywords
- Cyclic peptide
- Inhibititor
- Pargamicin
- PD124,966
- Poly(ADP-ribose) glycohydrolase
ASJC Scopus subject areas
- Agricultural and Biological Sciences(all)
- Physics and Astronomy(all)