Sequencing and synthesis of pardaxin, a polypeptide from the Red Sea Moses sole with ionophore activity

Yechiel Shai*, Jay Fox, Carlo Caratsch, Yu Liang Shih, Charles Edwards, Philip Lazarovici

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

109 Scopus citations

Abstract

Pardaxin, an amphipathic polypeptide secreted by the Red Sea flatfish Pardachirus marmoratus whose sequence is NH2-G-F-F-A-L-I-P-K-I-I-S-S-P-L-F-K-T-L-L-S-A-V-G-S-A-L-S-S-S-G-G-Q-E, was synthesized by the solid-phase method. The structure was verified by sequencing. The synthetic polypeptide changed the resistance of lipid bilayers by forming pores. At 10-7-10-8 M, the synthetic pardaxin increased the frequency of the spontaneous release of quanta of acetylcholine at the neuromuscular junction by up to 100-fold, resembling the native product. Synthetic pardaxin seems to be a suitable tool for investigating the molecular structures underlying channel selectivity.

Original languageEnglish
Pages (from-to)161-166
Number of pages6
JournalFEBS Letters
Volume242
Issue number1
DOIs
StatePublished - 19 Dec 1988
Externally publishedYes

Keywords

  • Neuromuscular junction
  • Pardaxin
  • Planar lipid bilayer
  • Pore activity
  • Presynaptic activity

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