Primary Structure of a Cardioactive Neuropeptide From the Tobacco Hawkmoth, Manduca Sexta

FEBS Lett. 1992 Nov 23;313(2):165-8. doi: 10.1016/0014-5793(92)81436-p.

Abstract

The amino acid sequence of the first of a family of insect cardioregulatory peptides from the tobacco hawkmoth, Manduca sexta, has been determined using a combination of Edman degradation microsequencing and mass spectroscopy. This peptide contains 9 amino acid residues and an observed mass for the monoisotopic protonated molecule of 956.4 Da. There are two cysteines at positions 3 and 9 forming a disulfide bridge and the carboxyl-terminus is amidated. The structure of this peptide, Pro-Phe-Cys-Asn-Ala-Phe-Thr-Gly-Cys-NH2, is identical to a peptide recently isolated from crabs called crustacean cardioactive peptide (CCAP) and we propose that this peptide be named Manduca CCAP.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Chromatography, High Pressure Liquid
  • Insect Hormones / chemistry*
  • Mass Spectrometry
  • Molecular Sequence Data
  • Moths / chemistry*
  • Oligopeptides / chemistry*
  • Pyrrolidonecarboxylic Acid / analogs & derivatives

Substances

  • Insect Hormones
  • Oligopeptides
  • adipokinetic hormone
  • Pyrrolidonecarboxylic Acid