Alpha-conotoxins act on postsynaptic membranes, they bind to the nicotinic acetylcholine receptors (nAChR) and thus inhibit them. This toxin selectively inhibits nicotinic acetylcholine receptor (nAChR) alpha-3-beta-2 subtype (IC(50)=845.5 nM). Expressed by the venom duct. The cysteine framework is I (CC-C-C). Alpha4/6 pattern. The toxin is inactive on the alpha-3-beta-2 nAChR when the disulfide bond connectivity is C1-C4 and C2-C3 (ViIA-I) (IC(50)>10000 nM). This toxin does not inhibit alpha-2-beta-2, alpha-2-beta-4, alpha-3-beta-4, alpha-4-beta-2, alpha-4-beta-4, alpha-7 and alpha-9-alpha-10 (PubMed:26511093). In addition, it does not target dorsal root ganglion sodium (Nav), potassium (Kv) and calcium (Cav) ion channels (PubMed:26511093). Belongs to the conotoxin A superfamily. Authors of PubMed:26511093 indicate an amidation at Cys-61. This amidation is improbable since no Gly follows the mature peptide region. This PTM is therefore not indicated here and we assume that electrophysiological results are obtained with an unamidated synthetic peptide.