Abstract
The conopeptides are the conotoxin ofConus loroisiihave wide applications in drug development. This work emphasizes the isolation and identification of conopeptides formConus loroisiiand the peptides were characterized using LC-MS/MS ESI fragmentation technique and showing 50 protein sequences with disulfide linkages of the molecular mass of 352-1263 m/z. The conotoxin peptide having O1, O2, M, S, I1, J, A and T-superfamily. The gel electrophoresis results also confirmed the protein bands above 20 kDa. The Fourier transform infrared (FT-IR) spectra reported the presence of halometabolites found in marine-derived conopeptides. Moreover, the toxicity of conopeptide has been studied with brine shrimps, chorioallantoic membrane, and breast cancer cell lines (MCF-7). The in-silico analysis of HPV protein databases reveals conotoxin protein has strong interactions and the toxicity assay proved that the conotoxin ofC. loroisiias a potential anti-cancer drug.