N-terminal portion of motilin determines its biological activity

Biochem Biophys Res Commun. 1992 Feb 28;183(1):36-40. doi: 10.1016/0006-291x(92)91605-p.


This study aimed to identify the portion of the 22 amino acid sequence of motilin responsible for the biological activity of the peptide. The contraction of rabbit duodenal muscle in vitro was measured when exposed to synthetic fragments of motilin corresponding to various sequences of the C- or N-terminal portions of the molecule. Fragments 2-22 or 3-22 (where the initial amino acids of the N-terminal ending were removed) were more than 1000 times less potent than the native molecule 1-22. Fragment 1-9 (where the last 13 amino acids located at the C-terminal side of motilin were removed) was devoid of any contractile capacity, while synthetic fragments whose C-terminal structure extended beyond the 1-9 motilin sequence maintained almost complete biological activity. N-terminal amino acid sequence 1-9 is therefore an essential determinant of the contractile activity of motilin.

MeSH terms

  • Animals
  • Binding Sites
  • Biological Assay
  • Duodenum / drug effects*
  • Motilin / chemical synthesis
  • Motilin / pharmacology*
  • Muscle Contraction / drug effects*
  • Peptide Fragments / chemical synthesis
  • Peptide Fragments / pharmacology*
  • Rabbits


  • Peptide Fragments
  • Motilin