Inclusion of a beta-aspartyl peptide bond causes the loss of inherent physiological activities

J Biochem. 1994 Jan;115(1):15-7. doi: 10.1093/oxfordjournals.jbchem.a124291.

Abstract

Growth-blocking peptide (GBP) is a peptide which was initially isolated from the plasma of last instar larvae of the insect armyworm, Pseudaletia separata, parasitized by the parasitoid wasp, Cotesia kariyai. A standard GBP acid, a free carboxyl terminal GBP, was synthesized by solid phase methods, using 7-fluorenylmethoxycarbonyl (Fmoc) and tert-butyloxycarbonyl (Boc) amino acids, respectively. The peptide synthesized using Boc amino acids gave the expected structure of GBP, while approximately 90% of the peptide synthesized using Fmoc amino acids was a peptide with a beta-aspartyl (Asp) bond at position 16. The peptide containing the beta-Asp bond does not exhibit any physiological effect on armyworm larvae.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Aspartic Acid / physiology*
  • Chromatography, High Pressure Liquid
  • Cytokines*
  • Insect Proteins*
  • Larva / growth & development
  • Molecular Sequence Data
  • Moths
  • Peptides / chemistry*
  • Peptides / physiology*
  • Structure-Activity Relationship

Substances

  • Cytokines
  • Insect Proteins
  • Peptides
  • growth blocking peptide, Apanteles kariyai
  • Aspartic Acid