Active fragments and analogs of the insect neuropeptide leucopyrokinin: structure-function studies

Biochem Biophys Res Commun. 1986 Jun 30;137(3):936-42. doi: 10.1016/0006-291x(86)90315-3.

Abstract

Evaluation of analogs of the blocked insect myotropic neuropeptide leucopyrokinin (LPK) has demonstrated its relative insensitivity to amino acid substitution in the N-terminal in contrast to the C-terminal region. Truncated analogs of LPK without the first, second, and third N-terminal amino acids retain a significant 144%, 59% and 30% of the activity of the parent octapeptide, respectively. The [2-8]LPK analog is the first fragment of an insect neuropeptide to exhibit greater activity than the parent hormone. In contrast, truncated analogs of the insect myotropic, proctolin, exhibit little or no activity. The pentapeptide fragment Phe-Thr-Pro-Arg-Leu-NH2 has been identified as the active core of LPK.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Cockroaches / physiology*
  • Gastrointestinal Motility
  • Insect Hormones* / physiology
  • Nerve Tissue Proteins* / physiology
  • Oligopeptides* / physiology
  • Peptide Fragments
  • Pyrrolidonecarboxylic Acid / analogs & derivatives
  • Receptors, Cell Surface / physiology
  • Structure-Activity Relationship

Substances

  • Insect Hormones
  • Nerve Tissue Proteins
  • Oligopeptides
  • Peptide Fragments
  • Receptors, Cell Surface
  • leucopyrokinin
  • Pyrrolidonecarboxylic Acid