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Publication Abstract from PubMed

Elevenins are peptides found in a range of organisms, including arthropods, annelids, nematodes, and molluscs. They consist of 17 to 19 amino acid residues with a single conserved disulfide bond. The subject of this study, elevenin-Vc1, was first identified in the venom of the cone snail Conus victoriae (Gen. Comp. Endocrinol. 2017, 244, 11-18). Although numerous elevenin sequences have been reported, their physiological function is unclear, and no structural information is available. Upon intracranial injection in mice, elevenin-Vc1 induced hyperactivity at doses of 5 or 10 nmol. The structure of elevenin-Vc1, determined using nuclear magnetic resonance spectroscopy, consists of a short helix and a bend region stabilised by the single disulfide bond. The elevenin-Vc1 structural fold is similar to that of alpha-conotoxins such as alpha-RgIA and alpha-ImI, which are also found in the venoms of cone snails and are antagonists at specific subtypes of nicotinic acetylcholine receptors (nAChRs). In an attempt to mimic the functional motif, Asp-Pro-Arg, of alpha-RgIA and alpha-ImI, we synthesised an analogue, designated elevenin-Vc1-DPR. However, neither elevenin-Vc1 nor the analogue was active at six different human nAChR subtypes (alpha1beta1epsilondelta, alpha3beta2, alpha3beta4, alpha4beta2, alpha7, and alpha9alpha10) at 1 microM concentrations.

Characterisation of Elevenin-Vc1 from the Venom of Conus victoriae: A Structural Analogue of alpha-Conotoxins.,Krishnarjuna B, Sunanda P, Seow J, Tae HS, Robinson SD, Belgi A, Robinson AJ, Safavi-Hemami H, Adams DJ, Norton RS Mar Drugs. 2023 Jan 25;21(2):81. doi: 10.3390/md21020081. PMID:36827123^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.