The Chemistry of Reptile Venom

Reptile venom is a complex mixture of different proteins that impacts specific regions and functions in prey. These toxins are injected from unique fangs during a snake bite. The venom also contains chemicals that protect snakes from threats.


Many venom compounds are being used as drugs to treat snake bites and conditions such as cancer, hypertension and thrombosis. These peptides are particularly valuable because of their diversified pharmacological properties and high affinity and selectivity towards their receptors.

Venoms are a natural gift

Venoms are natural gifts that help predators hunt and defend themselves. These bioactive cocktails, composed of proteins and peptides, are highly versatile weapons that impact specific regions and functions of the target body. However, venoms are often under-explored and remain poorly understood. Injections of snake venom drain the animal, which is why snakes only use their venom when they feel threatened or have a reason to defend themselves.

For example, venoms can be neurotoxic, hemotoxic or cytotoxic. Neurotoxic venoms can cause severe damage to the brain and nervous system, while hemotoxic venom affects blood cells. Cytotoxic venom kills the target cells and can also cause inflammation. The Black Mamba is said to be the deadliest snake in the world because of its venom, which has been proven to kill humans within 30 minutes.

Interestingly, venoms can differ between snake species even when they belong to the same genus. This is likely due to evolutionary and ecological factors. Moreover, venoms can also be influenced by the type of prey the snakes feed on.

The recent development of organoid culturing methods makes it possible to study venom glands from snakes and other venomous reptiles. These systems can maintain venom gland epithelia for up to a year, which is significantly longer than previously reported. This advancement could allow researchers to analyze the venom synthesis mechanisms of snakes, helodermatid lizards and monotremes in a much more detailed manner.

They are a weapon

Venoms are powerful weapons that can kill, incapacitate and paralyze taxa of prey species. They are composed of enzymes that damage innard tissues and the nervous system. They can also be used to defend snakes from predator species. Venom chemistry is partially understood, but more research at the atomic level is required to fully understand its bioactivity. This will be possible using new methods of determining the chemistry of complex chemical reactions, such as computational models and quantum mechanical simulations.

There is considerable variation in venom composition between snake species and within groups, such as viperids and elapids. Different venoms are designed to achieve specific functions, such as neurotoxic, hemotoxic and myotoxic effects. Moreover, the proportion and relative concentration of different protein families can also vary between individual snakes. This means that a treatment for snakebite must match the type of bite. For example, polyvalent antivenoms are available for the bites of pit vipers.

The venom is delivered by unique fangs during a bite, though some species are also able to spit venom when threatened or irritated. These venoms contain a variety of toxins that aid in the immobilization and digestion of prey, as well as defense against predators. While most textbooks claim that only a quarter of snakes are venomous, new discoveries are challenging this assumption. Scientists have discovered venom in the mouth glands of supposedly non-venomous species, such as the lace monitor and bearded dragon. The discovery of these toxins is causing a heated debate over the origins of reptilian venoms.

They are a tool

Venoms are used by snakes to subdue prey and to protect themselves. They are complex mixtures of enzymatic and non-enzymatic components that act mainly on ion channels or G-protein coupled membrane receptors as well as components of the blood clotting system. Peptide toxins found in animal venoms can target specific pathophysiological processes with high selectivity and affinity.

The venoms of viperid reptiles contain a large number of different protein families that differ significantly at the species level. Some of them are well-studied, such as the PLA2s, SVMPs and C-type lectins. Others, such as defensins, are less abundant and have a unique mode of action. Defensins bind to Na+ and K+ channels and accumulate in the lysosomes, where they cause analgesic, neurotoxic and myotoxic effects.

Snakes produce venom through a modified parotid salivary gland on each side of the head and deliver it into prey with specialised tubular fangs. These teeth have grooves or canals that guide the venom to the bite wound.

The venoms of viperid snakes contain nine major protein families, but there is substantial variation between venoms and even within a single species. Despite this diversity, the structures of most venom proteins are conserved and have similar folds. One example is the RVV-X metalloproteinase from the eastern Russell’s viper (Daboia siamensis). This enzyme hydrolyses the Arg194-Ile195 region of blood coagulation factor X, and its structure has been characterized.

They are dangerous

Snakes do not have claws or powerful jaws to pin down their prey, so they rely on venom to kill it. Their venoms contain a cocktail of enzymes and proteins that act in diverse ways to paralyse prey and injure the bite wound. They are often deadly, and their use is inherently dangerous.

Venom composition can vary widely across species, and within a species it can change with age, diet, and geographic location. The venoms of Russell’s vipers (Daboia russelii) and saw-scaled vipers (Echis carinatus) are two of the most lethal snakes in the world, with high rates of fatalities owing to their toxicity, discreet but aggressive habits, and widespread distribution in densely populated areas.

In addition to cytotoxic and hemotoxic components, venoms often contain proteolytic enzymes that destroy tissue structures in the bite wound. They work in conjunction with venom toxin to speed up the degradation of blood vessels and muscle tissue, enabling the prey to bleed out more quickly and aiding digestion.

Claude Bernard, the 19th-century father of experimental medical science, said that venoms are “veritable reagents of life, extremely delicate instruments which dissect vital units.” The wide utility of venom is now well established, but it is important to note that snake venoms are very dangerous. Even with the availability of antivenom, many people die from snake bites each year. More research and increased caution are needed to prevent these tragedies.