Structure-activity relationships in C-terminal fragment analogs of pheromone biosynthesis activating neuropeptide in Helicoverpa zea

Arch Insect Biochem Physiol. 1997;35(3):315-22. doi: 10.1002/(SICI)1520-6327(199705)35:3<315::AID-ARCH5>3.0.CO;2-S.

Abstract

A number of analogs of the C-terminal hexapeptide of PBAN were prepared and tested in vivo for pheromonotropic activity in Helicoverpa zea. Peptides prepared with longer-chain omega-aminocarboxylic acids (Tyr-6-aminocaproyl-Leu-NH2 and Tyr-7-aminoheptanoyl-NH2) were active at 25 and 2.5 nmol. Acetyl-Pro-Arg-Leu-NH2 was active at 1,000 pmol and represents a new minimum active fragment in the PBAN system. Addition of a bulky, hydrophobic tail (4-octylphenoxyacetyl) to the C-terminal hexapeptide of PBAN gave an analog that was active at all concentrations tested from 1 to 1,000 pmol when injected, had slight oral activity, but had no activity when applied topically. Glu-Tyr-Phe-Ser-Pro-Arg-Leu-NH2 was active at 1,000 but not at 100 pmol; at the latter dose it synergised the activity of 5 pmol of PBAN.

MeSH terms

  • Animals
  • Moths
  • Neuropeptides / chemistry
  • Neuropeptides / metabolism*
  • Peptide Fragments / chemistry
  • Peptide Fragments / metabolism
  • Sex Attractants / chemistry
  • Sex Attractants / metabolism*
  • Structure-Activity Relationship

Substances

  • Neuropeptides
  • Peptide Fragments
  • Sex Attractants
  • pheromone biosynthesis activating neuropeptide, Helicoverpa zea