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XB-ART-54376
Biochemistry 2017 Nov 14;5645:6051-6060. doi: 10.1021/acs.biochem.7b00485.
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Structure and Biological Activity of a Turripeptide from Unedogemmula bisaya Venom.

Omaga CA , Carpio LD , Imperial JS , Daly NL , Gajewiak J , Flores MS , Espino SS , Christensen S , Filchakova OM , López-Vera E , Raghuraman S , Olivera BM , Concepcion GP .


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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-NH 2 (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 α9α10 nicotinic acetylcholine receptor with relatively low affinity (IC 50 , 10.2 μM). Initial Constellation Pharmacology data revealed an excitatory activity of ubi3a on a specific subset of mouse dorsal root ganglion neurons.

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