A new peptide in the FMRFamide family isolated from the CNS of the hawkmoth, Manduca sexta

Timothy G. Kingan, David B. Teplow, Jessica M. Phillips, John P. Riehm, K. Ranga Rao, John G. Hildebrand, Uwe Homberg, Ann E. Kammer, Ian Jardine, Patrick R. Griffin, Donald F. Hunt

Research output: Contribution to journalArticlepeer-review

127 Scopus citations


We have purified a FMRFamide-like peptide from extracts of brain-subesophageal ganglion of the moth, Manduca sexta. The purification was monitored with a new, competitive ELISA, and accomplished with ion exchange and reverse-phase HPLC. The peptide structure was determined by a combination of tandem mass spectrometry and automated Edman degradation. The amino acid sequence of the peptide is <Glu-Asp-Val-Val-His-Ser-Phe-Leu-Arg-Phe-amide (pEDVVHSFLRF-NH2). In a separate purification, an identical peptide was isolated from extracts of brain-associated neurohemal structures. We have named this peptide ManducaFLRFamide, to indicate its homology with other members of the "FMRFamide" family. In bioassays, chemically synthesized peptide increased the force of neurally evoked contractions in the major power-producing flight muscles, the dorsal longitudinal muscles. This observation suggests that hormonally released ManducaFLRFamide may play a role in sustaining or promoting the flight behavior necessary for mate-seeking (in males) or oviposition (in females) in sphingid moths.

Original languageEnglish (US)
Pages (from-to)849-856
Number of pages8
Issue number4
StatePublished - 1990


  • FMRFamide family
  • HPLC
  • Hawkmoth
  • Ion exchange
  • Peptide purification

ASJC Scopus subject areas

  • Biochemistry
  • Physiology
  • Endocrinology
  • Cellular and Molecular Neuroscience


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