Synthetic study on the structure-activity relationship of sperm activating peptides from the jelly coat of sea urchin eggs

Biochem Biophys Res Commun. 1985 Jan 31;126(2):974-82. doi: 10.1016/0006-291x(85)90281-5.

Abstract

Various analogue peptides with substitution and deletion of amino acid residues have been synthesized by liquid phase method for Sperm Activating Peptides from the jelly coat of sea urchin eggs. The deletion of C-terminal Gly reduced the activity to about 1/3000, while removal of N-terminal Gly reduced the activity to 1/10. The residues Ser5 and Asp3 were replaced by Lys without significant loss of activity. Substitution of Phe2 by Gly, Ala or Pro markedly reduced the activity by the factor of 10(4)-10(6), in contrast to Tyr-substitution retaining almost full activity, indicating the essential role of the aromatic residue in exerting the activity. Substitutions, Asp3 to Glu and Gly10 to Pro, increased the activity 5-fold and 500-fold, respectively.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Chemical Phenomena
  • Chemistry
  • Chromatography, High Pressure Liquid
  • Egg Proteins / chemical synthesis*
  • Egg Proteins / physiology
  • Female
  • Male
  • Oligopeptides / chemical synthesis*
  • Oligopeptides / physiology
  • Sea Urchins
  • Spermatozoa / physiology*
  • Structure-Activity Relationship

Substances

  • Egg Proteins
  • Oligopeptides
  • speract