A novel peptide toxin, delta-conotoxin GmVIA, was purified from the venom of Conus gloriamaris, a mollusc-hunting snail. It consists of 29 amino acids, including six Cys residues: [sequence: see text] The pattern of disulfide connectivity (4-19, 12-24, and 18-29) is the same as for the omega-conotoxins, which are Ca2+ channel ligands. However, the peptide does not compete with omega-conotoxin for binding to membrane preparations from frog, rat, and chick brain. Instead, initial electrophysiological results suggest that the peptide induces action potential broadening in molluscan neurons by slowing down Na+ current inactivation. Synthetic delta-conotoxin GmVIA was prepared by solid-phase methods and appeared identical in all respects to the natural material. The chromatographic behavior of native and reduced delta-conotoxins is quite remarkable, suggesting that the disulfides form a core which forces hydrophobic residues to point out toward the solvent.