1Department of Microbiology, Shridevi Institute of Allied Health Sciences, Tumakuru, 572106, India
2Division of Biotechnology, School of Agricultural Sciences, Karunya Institute of Technology and Sciences, Karunya Nagar, Coimbatore, 641114, India
3Department of Environmental Science, School of Vocational Studies and Applied Sciences, Gautam Buddha University, Greater Noida, 201312, India
4Department of Mining Engineering, Indian Institute of Technology (Banaras Hindu University), Varanasi, 221005, India
5Lohum Cleantech Pvt. Ltd., Kasna Industrial Area, D-184, Site V, Greater Noida, 201306, India
6Department of Botany, Yuvaraja’s College, University of Mysore, Mysuru, 570005, India
7Sprott Centre for Stem Cell Research, Ottawa Hospital Research Institute, Ottawa, ON, K1Y 4E9, Canada
8Department of Chemistry, Karpaga Vinayaga College of Engineering and Technology, Chengalpattu, 603308, India
9Department of Biotechnology and Chemical Engineering, School of Civil and Chemical Engineering, Manipal University, Jaipur, Jaipur, 303007, India
10Department of Environmental Engineering and Management, Chaoyang University of Technology, Taichung, 413310, Taiwan
11Department of Bioengineering, Saveetha School of Engineering, Saveetha Institute of Medical and Technical Sciences, Chennai, 602105, India
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.
Venomous species, Peptide toxin, Neurological disorders, Intramolecular disulfide folds, Ion channels/receptors
