Inhibition of poly(ADP-ribose) glycohydrolase activity by cyclic peptide antibiotics containing piperazic acid residues

Mitsuko Masutani, Takashi Shimokawa, Masayuki Igarashi, Masa Hamada, Atsushi Shibata, Sachiho Oami, Tadashige Nozaki, Hitoshi Nakagama, Takashi Sugimura, Tomio Takeuchi, Makoto Hori

Research output: Contribution to journalArticlepeer-review

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 languageEnglish
Pages (from-to)15-17
Number of pages3
JournalProceedings of the Japan Academy Series B: Physical and Biological Sciences
Volume78
Issue number1
DOIs
Publication statusPublished - 2002 Jan
Externally publishedYes

Keywords

  • Cyclic peptide
  • Inhibititor
  • Pargamicin
  • PD124,966
  • Poly(ADP-ribose) glycohydrolase

ASJC Scopus subject areas

  • Agricultural and Biological Sciences(all)
  • Physics and Astronomy(all)

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