Identification of Neuroactive Peptide from Venomous Species using Structural Analysis: A Possible Neuronal Therapeutic Candidate

Neuroactive peptides derived from venomous species have proven to be used as a lead compound for treating neurological diseases. In the present study, the primary structure of the peptide toxins of snakes, scorpions, spiders, cone snails, honey bees, and sea anemones was recovered from different toxin databases. The 3-D structures of the peptide toxins were analyzed with respect to secondary structural elements such as cysteine patterns and disulfide connectivity’s using PYMOL. Their interaction with ion channels/receptors was studied because of its pharmacological importance. The toxins retrieved were found to have – C–Xn–C–Xn–CC–Xn–C–Xn–C-- cysteine pattern for n≥1 that was the same --C---C---CC---C---C— cysteine pattern of ω-conotoxin and hanatoxin, but with a varying intervening non-cysteine residue between cysteines. Hence, these provide insight for structure-based drug design using these peptide toxin scaffolds. Given the optimal molecular weight and specificity of peptides compared to conventional small molecule drugs, peptides are considered future next-generation drug candidates.