Pharmacologically active peptides that may have analgesic applications have been discovered and have since been widely studied in marine gastropods, particularly those belonging to the Turridae family. Several studies have worked on expressing Turrid peptides in bacteria followed by several in vivo mouse assays to test for bioactivity. However, optimum peptide action depends on proper peptide folding and the post translation modifications in the mature protein. Studies have shown that post-translational modifications in insect cells are highly similar to those in mammalian cells. In this study, putative venomous peptides from the splendid gem turrid snail, Gemmula speciosa (Gsp), are expressed in Spodoptera frugiperda (Sf9) pupal ovarian cells through a baculovirus expression system. Peptides are purified through column chromatography, with further characterization through mass spectrometry. Purified peptides are screened for neuroactivity through intracranial and intrathecal injections in mice, followed by the tail flick assay and the hot plate test. In this paper, we present the results of our recombinant expression system and compare these with those obtained using synthetic peptides.