Solution structure of paralytic peptide of silkworm, Bombyx mori

Kazunori Miura, Manabu Kamimura, Tomoyasu Aizawa, Makoto Kiuchi, Yoichi Hayakawa, Mineyuki Mizuguchi, Keiichi Kawano*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

24 Scopus citations

Abstract

Paralytic peptide of Bombyx mori (BmPP) is one of the multifunctional ENF-peptides; the name of "ENF" is the consensus N-terminal amino acid sequence of the family peptides. We revealed that BmPP significantly possesses growth-blocking activity and plasmatocyte-spreading activity and that its activity profiles are different from those of another ENF-family peptide, namely, the growth-blocking peptide of Pseudaletia separata (PsGBP). We also determined the NMR structures of BmPP and PsGBP under the same conditions, which revealed the structural differences of the first and second β-turn regions between the two peptides. On the basis of our results, it can be considered that the tertiary structural difference in these peptides may cause their different profiles of growth-blocking activity.

Original languageEnglish
Pages (from-to)2111-2116
Number of pages6
JournalPeptides
Volume23
Issue number12
DOIs
StatePublished - 2002/12/01

Keywords

  • BmPP
  • Bombyx mori
  • Growth-blocking activity
  • Nuclear magnetic resonance
  • Paralytic peptide
  • Plasmatocyte-spreading activity
  • Solution structure

ASJC Scopus subject areas

  • Biochemistry
  • Physiology
  • Endocrinology
  • Cellular and Molecular Neuroscience

Fingerprint

Dive into the research topics of 'Solution structure of paralytic peptide of silkworm, Bombyx mori'. Together they form a unique fingerprint.

Cite this