δ-Conotoxin GmVIA, a Novel Peptide from the Venom of Conus gloriamaris

Ki Joon Shon, Lourdes J. Cruz, William R. Gray, Baldomero M. Olivera*, Arik Hasson, Micha E. Spira, Arik Hasson, Micha E. Spira

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

99 Scopus citations

Abstract

A novel peptide toxin, δ-conotoxin GmVIA, was purified from the venom of Conus gloriamaris, a mollusc-hunting snail. It consists of 29 amino acids, including six Cys residues: [formula omitted] The pattern of disulfide connectivity (4–19, 12–24, and 18–29) is the same as for the ω-conotoxins, which are Ca2+ channel ligands. However, the peptide does not compete with ω-conotoxin for binding to membrane preparations from frog, rat, and chick brain. Instead, initial electrophysiological results suggest that the peptide induces action potential broadening in molluscan neurons by slowing down Na+ current inactivation. Synthetic δ-conotoxin GmVIA was prepared by solid-phase methods and appeared identical in all respects to the natural material. The chromatographic behavior of native and reduced δ-conotoxins is quite remarkable, suggesting that the disulfides form a core which forces hydrophobic residues to point out toward the solvent.

Original languageEnglish
Pages (from-to)11420-11425
Number of pages6
JournalBiochemistry
Volume33
Issue number38
DOIs
StatePublished - 1 Sep 1994

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