New Perspectives on Snake Toxinology for Biotechnological Applications: a Narrative Review

Introduction: Snake venoms are evolutionarily shaped molecular libraries of enzymes, peptides and proteins. Toxinology has focused on envenoming and polyclonal antivenoms, whereas omics, protein engineering, structural bioinformatics and materials science enable broader biotechnological uses, yet their maturity has not been integratively appraised.

Objectives: To reposition snake toxins as biotechnological platforms (catalysts, scaffolds, engineering templates) and to grade the maturity of supporting evidence.

Methods: A narrative review of PubMed, Scopus and Web of Science (2020 - October 2026) included recent peer-reviewed studies and landmark earlier works, excluding outdated, flawed or off-topic ones. Evidence was graded as in silico/in vitro, animal or clinical/industrial.

Results: Snake venom enzymes act as catalytic scaffolds: immobilized PLA₂ cut phosphorus in soybean oil from 168 to <10 mg/kg, meeting refining requirements, and LAAOs converted L-methionine to its α-keto acid in batch. However, LAAO lost activity in continuous operation, PLA₂ discriminated poorly between enantiomers (E=3) and a bacterial LAAO showed higher affinity for L-DOPA, so these enzymes are versatile but not yet competitive, and selectivity and stability call for directed evolution and activity-verified recombinant supply. Pharmacologically, captopril and tirofiban show that toxin motifs become drugs once redesigned, whereas mined antimicrobial, anticancer and cell-penetrating peptides often show weak, mostly in vitro activity and some datasets include non-snake venoms, so they are templates for optimizing potency and selectivity. Venomics reveals geographic variation limiting antivenom coverage, while structural modeling enabled de novo binders and a nanobody cocktail neutralizing 17 of 18 African elapid venoms in mouse pre-incubation tests, suggesting defined recombinant molecules may replace polyclonal serum pending clinical validation. Biosensors, fibrin matrices and venom-gland organoids extend toxins to detection, materials and research, yet remain experimental. Limitations include scarce biocatalysis data and scale-up; integrating omics, structural design and benchmarked recombinant production is the way forward.

Conclusion: Snake toxins emerge as platforms of uneven maturity: antivenoms are closest to application, whereas catalysts and peptides require engineering.