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Isolation, primary structure and synthesis of neomyosuppressin, a myoinhibiting neuropeptide from the grey fleshfly, Neobellieria bullata.

Authors
  • Fónagy, A
  • Schoofs, L
  • Proost, P
  • Van Damme, J
  • Bueds, H
  • De Loof, A
Type
Published Article
Journal
Comparative biochemistry and physiology. C, Comparative pharmacology and toxicology
Publication Date
Jun 01, 1992
Volume
102
Issue
2
Pages
239–245
Identifiers
PMID: 1358537
Source
Medline
License
Unknown

Abstract

1. An amidated decapeptide, showing strong inhibitory activity of spontaneous visceral muscle movement was isolated, from head extracts of 42 thousand fleshflies, Neobellieria bullata (Diptera, Sarcophagidae). 2. Amino acid sequencing and verification by peptide synthesis revealed the following primary structure: Thr-Asp-Val-Asp-His-Val-Phe-Leu-Arg-PheNH2. 3. The novel peptide was termed neomyosuppressin or Neb-MS. 4. During the process of consecutive high performance liquid chromatography (HPLC) purifications the biological activity of the samples was monitored using heterologous bioassay system. 5. The threshold level of synthetic Neb-MS was found to be 8.6 +/- 0.5 x 10(-11) M on the Leucophaea hindgut and 3.4 +/- 0.5 x 10(-10) M on the Locusta oviduct bioassay, respectively.

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