Therapeutic Potential of Venom Peptides (Chapter 16)



The biochemical composition of animal venoms (scorpions, snakes, spiders, cone snails, etc.) is diverse and contains short and large proteins with neurotoxic and enzymatic activities. Some short peptides act specifically to discriminate among Ca2+, Na+, and K+ ion channel subtypes, or act as inhibitors or activators of receptors that in turn could affect human physiology. Their selective affinities for ion channel subfamilies are also functional for mapping excitable cells. Furthermore, several of these short peptides have been proved to hyperpolarize peripheral neurons, which are associated with supplying sensation to the skin and skeletal muscles. For instance, some spider N-type calcium ion channel blockers may be important for the treatment of chronic pain. A special group of spider peptides are amphipathic and positively charged peptides. Their secondary structure is alpha-helical, and they insert into the lipid cell membrane of eukaryotic or prokaryotic cells leading to the formation of pores and subsequently depolarizing the cell membrane. Venom peptides from animal venoms represent an interesting source of molecules for the design of novel pharmaceutical drugs. This chapter presents the therapeutic properties of venom toxins and discusses the latest biochemical and molecular advances in the development of new therapies.  

Gbadamosi, Alaba & Ajayi, Abiola. (2023). Recent Advances in Molecular Biology and Biochemistry Relationships Among Gene Expression Profiles and Stress Tolerance Indices of Morphological Traits of Accessions of Cowpea Screened Under Differential Drought Stress Alaba Emmanuel Gbadamosi, Abiola Toyin Ajayi. ResearchGate Link to PDF (Book)