A novel 13 residue acyclic peptide from the marine snail, Conus monile, targets potassium channels
peer-reviewed · Biochemical and Biophysical Research Communications · 2004
| Date | 2004-05-01 |
| Type | peer-reviewed |
| Venue | Biochemical and Biophysical Research Communications |
| Publisher | Elsevier BV |
| Contribution | downstream-application |
| DOI | 10.1016/j.bbrc.2004.03.100 |
Abstract
A novel 13-residue peptide Mo1659 has been isolated from the venom of a vermivorous cone snail, Conus monile. HPLC fractions of the venom extract yielded an intense UV absorbing fraction with a mass of 1659Da. De novo sequencing using both matrix assisted laser desorption and ionization and electrospray MS/MS methods together with analysis of proteolytic fragments successfully yielded the amino acid sequence, FHGGSWYRFPWGY-NH(2). This was further confirmed by comparison with the chemically synthesized peptide and by conventional Edman sequencing. Mo1659 has an unusual sequence with a preponderance of aromatic residues and the absence of apolar, aliphatic residues like Ala, Val, Leu, and Ile. Mo1659 has no disulfide bridges distinguishing it from the conotoxins and bears no sequence similarity with any of the acyclic peptides isolated thus far from the venom of cone snails. Electrophysiological studies on the effect of Mo1659 on measured currents in dorsal root ganglion neurons suggest that the peptide targets non-inactivating voltage-dependent potassium channels.
Methods and tools
- Conus monile acyclic peptide Mo1659: De novo sequences Mo1659, a 13-residue disulfide-free aromatic peptide from Conus monile venom, from MALDI and ESI MS/MS, confirms it by synthesis and Edman sequencing, and shows it targets non-inactivating potassium channels.