Cone snails are members of the vast Conoidean group of venomous marine gastropods found in a variety of tropical and subtropical ocean ecosystems. They use their venom, like other venomous species, as a defensive mechanism as well as a tool for capturing their prey. As part of their neurochemical and biochemical strategy for catching prey, these species produce peptides that target specific ion channels and receptors, and they appear to have produced conotoxin, an unusual combination of pharmacologically active peptides. These conotoxins contain more than 100 components, resulting in a variety of active mono peptides used pharmacologically. However, studies on the structure of these peptides are still limited, leaving us with a gap in understanding their action, selectivity, and potency. Therefore, in silico and homology modeling studies on one (1) family of alpha-conotoxin from selected vermivorous Conus species were discussed in this study. The majority of the alpha-conotoxins were highly basic in nature, according to physicochemical characterization, with one alpha-conotoxin sequence (α-conotoxin Lt28.1) indicating acidic in nature. The index of instability ranges from stable α-conotoxin RgIA (14.62) to unstable α-conotoxin ImII (126.91). Additionally, the aliphatic index for the protein sequences studied ranges from 29.15 to 97.50, indicating that it is thermostable over a wide temperature range. Furthermore, GRAVY values for alphaconotoxins range from -0.910 (most hydrophilic; α-conotoxin SrIA/SrIB) to 0.731 (most hydrophobic; alphaconotoxin Lp1.1). Moreover, toxin_8 was discovered to be the common domain among the species. A random coil dominates other secondary structures in terms of percentage score of amino acid distribution for secondary structure prediction, followed by α-helix, β-strand, and β-turns. Finally, the predicted models for α-conotoxin Lp1.4, α-conotoxin ArIA, α-conotoxin VxXXC, α-conotoxin VxXXA, and α-conotoxin LvIA are of high quality, with ≥ 90% coverage in their favored regions.