Isolation and identification of a new diuretic peptide from the tobacco hornworm, Manduca sexta

Biochem Biophys Res Commun. 1991 Dec 31;181(3):927-32. doi: 10.1016/0006-291x(91)92025-f.


A 30-amino acid diuretic peptide was isolated from the corpora cardiaca-corpora allata complexes and, separately, from medial neurosecretory cells of the Sphingid moth, Manduca sexta. The peptide was found to have the following sequence, determined by automated Edman degradation and mass spectrometry: SFSVNPAVDILQHRYMEKV AQNNRNFLNRV-NH2. We have named the peptide Mas-DP II. The peptide was synthesized and shown to possess diuretic activity in decapitated moths. Mas-DP II is related by sequence homology to a 41-amino acid diuretic peptide identified previously from M. sexta, and it belongs to the family of corticotropin releasing factor-like peptides.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Chromatography, High Pressure Liquid
  • Diuresis / drug effects*
  • Female
  • Insect Hormones / chemical synthesis
  • Insect Hormones / isolation & purification*
  • Insect Hormones / pharmacology
  • Intercellular Signaling Peptides and Proteins
  • Male
  • Molecular Sequence Data
  • Moths / physiology*
  • Peptides*
  • Sequence Homology, Nucleic Acid


  • Insect Hormones
  • Intercellular Signaling Peptides and Proteins
  • Peptides
  • Mas-DP II