In silico analysis of κ-theraphotoxin-Cg2a from Chilobrachys guangxiensis

458-466κ-theraphotoxin-Cg2a is a 29- residue polypeptide extracted from the venomous glands of the Chinese earth tiger tarantula Chilobrachys guangxiensis. Plethoras of cancers are being associated with irregular functions of potassium ion channels. An extensive understanding of the toxin’s interaction with the voltage-gated potassium channels is of utmost necessity for it to be screened as a potential pharmacological molecule which may perhaps serve as toxin-based therapy to manage various cancer channelopathies. Physicochemical properties were studied, the evolutionary analysis was done to visualize the conserved domain among different toxins of tarantula family, docking studies between κ -theraphotoxin-Cg2a and a voltage-gated potassium ion channel was done by ClusPro 2.0. The presence of signal peptide was observed using PSIPRED. Cysteine – disulfide bonds present in the amino acid sequence was predicted by DiANNA server. Multiple sequence alignment illustrated conserved residues with other families of tarantula’s toxin. The docking of κ -theraphotoxin- Cg2a with the voltage-gated potassium channel was found to be interactive. The presence of cysteine –disulfide bonds were observed potentially playing a crucial role in the docking process. The interaction between the receptor and the ligand was found to be interactive which could turn out to help develop strategies to assist in creating potential pharmacological drug- based therapies