Apamin Apamin Apamin is an 18 amino acid peptide neurotoxin found in apitoxin (bee venom). Dry bee venom consists of 2–3% of apamin. Apamin selectively blocks SK channels, a type of Ca-activated K channel expressed in the central nervous system. Toxicity is caused by only a few amino acids, these are cysteine, lysine, arginine, arginine and histidine. These amino acids are involved in the binding of apamin to the Ca-activated K channel. Due to its specificity for SK channels, apamin is used as a drug in biomedical research to study the electrical properties of SK channels and their role in the
Evolution of snake venom highly venomous caenophidian snakes (also referred to as "colubroidian snakes"), thus suggesting that most venom evolution took place after this lineage diverged from other snakes. The primary mechanism for the diversification of venom is thought to be the duplication of gene coding for other tissues, followed by their expression in the venom glands. The proteins then evolved into various venom proteins through natural selection. This process, known as the birth-and-death model, is responsible for several of the protein recruitment events in snake venom. These duplications occurred in a variety of tissue types with a number of ancestral functions. Notable examples