Integrated Venomics Profiling of Apis dorsata and Vespa sp . Venoms Reveal Putative Bioactive Candidates

Apis dorsata and Vespa sp. venoms represent underexplored Hymenopteran bioresources with potential chemical and peptide diversity relevant to antimicrobial, cytoregulatory, and enzyme-target discovery. This exploratory venomics study generated a molecular profile comprising 510 metabolite features and 118 peptides/proteins, including 29 curated metabolite annotations and seven venom-associated peptide/protein classes supported by spectral evidence, database matching, and literature-supported curation. Major metabolite classes included lipids, hydrocarbons, heterocyclic compounds, fatty acids, phenols, terpenoids, esters, and amino acid/peptide-related metabolites. Proteomic profiling identified melittin, apamin, phospholipase A2, hyaluronidase, lysozyme, chymotrypsin inhibitor, and Kazal-like proteins in A. dorsata, while comparative Vespa sp. proteomics revealed homology-supported PLA1/PLA2-like proteins, DPP4-like proteins, serpins, PNGase, and QPCT. Exploratory co-abundance mapping suggested possible relationships among antioxidant triterpenoids, immune-regulating enzymes, neuropeptides, and lipid-associated venom components. Docking indicated preliminary interactions of vorinostat with Histone Deacetylase (HDAC) and adipostatin derivatives with Fatty Acid Synthase (FASN). Overall, this study prioritizes putative bioactive metabolites, venom-associated proteins, and predicted peptide candidates for future biochemical and functional validation.