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A novel contoxin inhibitor of Kv 1.6 channel and nicotinic acetylcholine receptor (nACHR) subtypes are used to define a new family of conotoxins, named p114a that has a potent activity at the nACHR subtypes, as well as the voltage-gated potassium channel subtype. The results show that there exist many similarities between the middle loop of p114a and the second loop of many other conotoxins though it is the first conotoxin to affect both the activities simultaneously.

Newly identified alphaA(sub s)-conotoxins was characterized from Conus pergrandis and a detailed characterization of alphaA-conotoxins was reported. The characterization of short alphaA-conotoxins revealed diverse kinetics of a block of the fetal muscle mammalian neuromuscular nicotinic acetylcholine receptor, particularly in dissociation rates.

A new approach is described that is employed for an efficient NMR-based mapping of the disulfide bridges in cysteine-rich peptides. The application of the method to the three-disulfide-bridged conotoxin, [mu]-conotoxin SxIIIA is shown to be extremely effective and efficient.

The importance of hydroxypyrolines (Hyp) in the in vitro oxidative folding and biological activity of conotoxins is discussed. The results suggest that proline hydroxylation is very important in the structure and function of all the proteins and peptides.

The purification and biochemical characterization of a novel peptide, de13a, from the venom of the worm-hunting snail Conus delessertii is described. The peptide is the first example of a novel conotoxin superfamily and the first reported with Hyl.