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 40μg/ml. A novel cyclic peptide, pargamicin, isolated from a fermentation broth of Amicolatopsis sp., also inhibited Parg with IC50 of 28μg/ml. A linear peptide containing piperazic acid residues, piperastatin A, isolated from Streptomyces lavendofoliae, did not inhibit Parg activity.
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