Minimum structure of diapause hormone required for biological activity

Biosci Biotechnol Biochem. 1998 Oct;62(10):1875-9. doi: 10.1271/bbb.62.1875.

Abstract

Diapause hormone is a 24-amino acid peptide amide, and its C-terminal penta-peptide amide structure of FGPRL-NH2 is believed to be essential for biological activity. The penta-peptide amide, the shorter peptide amides, and their derivatives and analogs were prepared to determine the minimal structure for biological activity. The C-terminal amide group of penta-peptide amide was not replaced with the other functional groups, but Gly, the 4th amino acid from the C terminal, could be substituted with an other amino acid while maintaining the biological activity. The shorter peptide amide, PRL-NH2, possessed low but significant activity, indicating the minimum structure of diapause hormone. By modifying its N-terminal, the aromatic ring of Phe is shown to enhance the activity of PRL-NH2.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Bombyx / drug effects
  • Bombyx / metabolism*
  • Dose-Response Relationship, Drug
  • Neuropeptides / chemistry*
  • Neuropeptides / pharmacology
  • Oligopeptides / chemical synthesis
  • Oligopeptides / pharmacology
  • Structure-Activity Relationship

Substances

  • Neuropeptides
  • Oligopeptides
  • phenylalanyl-glycyl-prolyl-arginyl-leucinamide
  • diapause hormone