Venom Peptides from Terrestrial Species

Venom peptides from terrestrial species, particularly those from snakes, spiders, scorpions, and insects, have garnered significant attention due to their potent biological activities. These peptides, which are part of a complex venom mixture, are designed to immobilize prey or defend against predators by targeting critical physiological systems, such as the nervous system or blood clotting mechanisms. Venom peptides from terrestrial species exhibit a wide range of pharmacological properties, making them promising candidates for therapeutic applications, including pain management, cardiovascular disease treatment, and antimicrobial therapies.¹

Mechanisms of Action

The mechanisms by which terrestrial venom peptides exert their effects are diverse and often highly specific. Many peptides from snake venoms act as neurotoxins, binding to ion channels or receptors on nerve cells, leading to paralysis or death in prey. For instance, peptides like α-bungarotoxin, found in the venom of the banded krait, Bungarus multicinctus, bind irreversibly to nicotinic acetylcholine receptors, preventing nerve signal transmission.² Similarly, some scorpion venom peptides, such as those from Leiurus quinquestriatus, target voltage-gated sodium channels, NaV, to disrupt neuronal signaling, causing paralysis.³

Therapeutic Applications

Venom peptides from terrestrial species are increasingly being explored for their therapeutic potential. For example, ziconotide, derived from the venom of the cone snail, Conus magus, is a synthetic peptide that acts as a calcium channel blocker and is used to treat severe chronic pain. Other terrestrial venom peptides, such as batroxobin from the venom of the lancehead viper, Bothrops atrox, are being developed as anticoagulants for managing blood clotting disorders.⁴

Challenges in Drug Development

Despite the promise of terrestrial venom peptides in drug development, several challenges exist. One major issue is peptide stability in the body, as venom peptides are often susceptible to degradation by proteases. Additionally, the specificity of venom peptides can pose a challenge in ensuring that they target the intended cells or tissues without causing off-target effects. Ongoing research focuses on peptide engineering to improve stability, bioavailability, and specificity.⁵

Citations

1. King, Glenn F. “Venoms to Drugs: Translating Venom Peptides into Therapeutics.” Toxicon, vol. 89, 2014, pp. 287–307. doi:10.1016/j.toxicon.2014.06.016.

2. Changeux, Jean-Pierre, and Thany, Steeve H. “Venom Toxins and Nicotinic Acetylcholine Receptors.” Biochemical Pharmacology, vol. 82, no. 6, 2011, pp. 904–917. doi:10.1016/j.bcp.2011.06.050.

3. Rodríguez de la Vega, Ricardo C., and Possani, Lourival D. “Current Views on Scorpion Toxins Specific for K+ Channels.” Toxicon, vol. 43, no. 8, 2004, pp. 865–875. doi:10.1016/j.toxicon.2004.03.005.

4. Miljanich, Gerard P. “Ziconotide: Neuronal Calcium Channel Blocker for Treating Severe Chronic Pain.” Current Medicinal Chemistry, vol. 11, no. 23, 2004, pp. 3029–3040. doi:10.2174/0929867043364177.

5. Craik, David J., and Adams, David J. “Venom Peptides as Therapeutics: Beyond Pain and Paralysis.” Bioorganic & Medicinal Chemistry, vol. 25, no. 21, 2017, pp. 4762–4772. doi:10.1016/j.bmc.2017.07.029.