Publication Type : Journal Article
Publisher : {FEBS} Letters
Source : \{FEBS\} Letters, Volume 553, Number 1–2, p.209 - 212 (2003)
Url : http://www.sciencedirect.com/science/article/pii/S0014579303010160
Keywords : Conus amadis
Campus : Amritapuri
School : School of Biotechnology
Center : Biotechnology
Department : biotechnology
Year : 2003
Abstract : A 26 residue peptide (Am 2766) with the sequence CKQAGESCDIFSQNCCVG-TCAFICIE-NH2 has been isolated and purified from the venom of the molluscivorous snail, Conus amadis, collected off the southeastern coast of India. Chemical modification and mass spectrometric studies establish that Am 2766 has three disulfide bridges. C-terminal amidation has been demonstrated by mass measurements on the C-terminal fragments obtained by proteolysis. Sequence alignments establish that Am 2766 belongs to the δ-conotoxin family. Am 2766 inhibits the decay of the sodium current in brain rNav1.2a voltage-gated Na+ channel, stably expressed in Chinese hamster ovary cells. Unlike δ-conotoxins have previously been isolated from molluscivorous snails, Am 2766 inhibits inactivation of mammalian sodium channels.
Cite this Research Publication : S. Sudarslal, Majumdar, S., Ramasamy, P., Dhawan, R., Pal, P. P., Ramaswami, M., Lala, A. K., Sikdar, S. K., Sarma, S. P., Krishnan, K. S., and Balaram, P., “Sodium Channel Modulating Activity in a δ-Conotoxin from an Indian Marine Snail”, \{FEBS\} Letters, vol. 553, pp. 209 - 212, 2003