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Publication Type : Journal Article
Publisher : Biochemical and Biophysical Research Communications
Source : Biochemical and Biophysical Research Communications, Volume 317, Number 3, p.682 - 688 (2004)
Url : http://www.sciencedirect.com/science/article/pii/S0006291X04005741
Keywords : Non-inactivating voltage-dependent potassium channel
Campus : Amritapuri
School : School of Biotechnology
Center : Biotechnology
Department : biotechnology
Year : 2004
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 1659nbsp;Da. 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-NH2. 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.
Cite this Research Publication : S. Sudarslal, Singaravadivelan, G., Ramasamy, P., Ananda, K., Sarma, S. P., Sikdar, S. K., Krishnan, K. S., and Balaram, P., “A Novel 13 Residue Acyclic Peptide from the Marine Snail, Conus Monile, Targets Potassium Channels”, Biochemical and Biophysical Research Communications, vol. 317, pp. 682 - 688, 2004