RgIA

**RgIA** is a disulfide-rich peptide toxin, specifically an **α-conotoxin**, isolated from the venom of the carnivorous marine cone snail *Conus regius*. It acts as a potent and selective antagonist of the **α9α10 nicotinic acetylcholine receptor (nAChR)**, blocking this receptor subtype with high affinity, particularly in its optimized variant RgIA4 for human receptors. Developed as a non-opioid analgesic, RgIA demonstrates efficacy in preclinical models of neuropathic pain, including nerve injury-induced and chemotherapy-induced (e.g., oxaliplatin) pain, by inhibiting α9α10 nAChR-mediated nociceptive signaling. Its rigid structure, maintained by two disulfide bonds, is critical for activity, though analogues like RgIA-5524 incorporate methylene thioacetal stabilizers for enhanced serum stability and clinical potential without compromising potency (IC50 ~1-10 nM).[1][2]

Other names

α-Conotoxin RgIA