The project focuses on the characterization and exploration of the bioactive components of Androctonus mauritanicus scorpion venom, with an emphasis on proteomic profiling and peptide identification. The overarching goal is to generate a comprehensive dataset of venom peptides and proteins, which can serve as a resource for understanding venom composition, discovering novel bioactive molecules, and facilitating comparative analyses with other scorpion species. Specimens were collected from a high-risk region for scorpion envenomation and maintained under controlled laboratory conditions. Venom was extracted via low-voltage electrical stimulation, centrifuged to remove impurities, lyophilized, and stored at −80°C to preserve biological activity. The venom was then solubilized, desalted, and fractionated using solid-phase extraction and reverse-phase high-performance liquid chromatography, allowing for separation of complex protein mixtures into manageable fractions suitable for mass spectrometry analysis. Enzymatic digestion was performed using trypsin and Lys-C, following reduction and alkylation steps to break disulfide bonds and prevent their reformation. Peptide samples were concentrated and analyzed using high-resolution mass spectrometry, including both Quadrupole Time-of-Flight (Q-TOF) and Orbitrap Q-Exactive platforms, coupled with nano-flow liquid chromatography. Data-dependent acquisition strategies were employed to maximize peptide coverage, and advanced software tools were used to process raw spectra, identify peptide sequences, and annotate post-translational modifications. The resulting dataset provides high-confidence peptide identifications, including sequence information suitable for deposition in public proteomics repositories. By sharing these data through ProteomeXchange, the project aims to enhance reproducibility, enable comparative studies, and support further research into venom-derived bioactive compounds with potential therapeutic applications.