Omaga, Carla, Carpio, Louie D., Imperial, Julita S., Daly, Norelle L., Gajewiak, Joanna, Flores, Malem S., Espino, Samuel S., Christensen, Sean, Filchakova, Olena M., López-Vera, Estuardo, Raghuraman, Shrinivasan, Olivera, Baldomero M., and Concepcion, Gisela P. (2017) Structure and biological activity of a turripeptide from Unedogemmula bisaya venom. Biochemistry, 56 (45). pp. 6051-6060.

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Abstract

The turripeptide ubi3a was isolated from the venom of the marine gastropod Unedogemmula bisaya, family Turridae, by bioassay-guided purification; both native and synthetic ubi3a elicited prolonged tremors when injected intracranially into mice. The sequence of the peptide, DCCOCOAGAVRCRFACC-NH2 (O = 4-hydroxyproline) follows the framework III pattern for cysteines (CC-C-C-CC) in the M-superfamily of conopeptides. The three-dimensional structure determined by NMR spectroscopy indicated a disulfide connectivity that is not found in conopeptides with the cysteine framework III: C-1-C-4, C-2-C-6, C-3-C-5. The peptide inhibited the activity of the alpha 9 alpha 10 nicotinic acetylcholine receptor with relatively low affinity (IC50, 10.2 mu M). Initial Constellation Pharmacology data revealed an excitatory activity of ubi3a on a specific subset of mouse dorsal root ganglion neurons.

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