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J. Biol. Chem., Vol. 275, Issue 42, 32391-32397, October 20, 2000

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Isolation and Characterization of a Novel Conus Peptide with Apparent Antinociceptive Activity^*

J. Michael McIntosh^§¶, Gloria O. Corpuz^§, Richard T. Layer, James E. Garrett, John D. Wagstaff, Grzegorz Bulaj^§, Alexandra Vyazovkina^§, Doju Yoshikami^§, Lourdes J. Cruz^§**, and Baldomero M. Olivera^§

From the Departments of  Psychiatry and ^§ Biology, University of Utah, Salt Lake City, Utah 84112,  Cognetix, Inc., Salt Lake City, Utah, 84108, and ^** Marine Science Institute, University of the Philippines, Diliman, Quezon City 1101, Phillipines

Cone snails are tropical marine mollusks that envenomate prey with a complex mixture of neuropharmacologically active compounds. We report the discovery and biochemical characterization of a structurally unique peptide isolated from the venom of Conus marmoreus. The new peptide, mr10a, potently increased withdrawal latency in a hot plate assay (a test of analgesia) at intrathecal doses that do not produce motor impairment as measured by rotarod test. The sequence of mr10a is NGVCCGYKLCHOC, where O is 4-trans-hydroxyproline. This sequence is highly divergent from all other known conotoxins. Analysis of a cDNA clone encoding the toxin, however, indicates that it is a member of the recently described T-superfamily. Total chemical synthesis of the three possible disulfide arrangements of mr10a was achieved, and elution studies indicate that the native form has a disulfide connectivity of Cys1-Cys4 and Cys2-Cys3. This disulfide linkage is unprecedented among conotoxins and defines a new family of Conus peptides.

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