Structure and Biological Activity of a Turripeptide from Unedogemmula bisaya Venom

Carla A. Omaga, Louie D. Carpio, Julita S. Imperial, Norelle L. Daly, Joanna Gajewiak, Malem S. Flores, Samuel S. Espino, Sean Christensen, Olena M. Filchakova, Estuardo López-Vera, Shrinivasan Raghuraman, Baldomero M. Olivera, Gisela P. Concepcion

Research output: Contribution to journalArticlepeer-review

3 Citations (Scopus)


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: C1-C4, C2-C6, C3-C5. The peptide inhibited the activity of the α9α10 nicotinic acetylcholine receptor with relatively low affinity (IC50, 10.2 μM). Initial Constellation Pharmacology data revealed an excitatory activity of ubi3a on a specific subset of mouse dorsal root ganglion neurons.

Original languageEnglish
Pages (from-to)6051-6060
Number of pages10
Issue number45
Publication statusPublished - Nov 14 2017

ASJC Scopus subject areas

  • Biochemistry

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