Reptile venom is a lethal secretion that has been fine-tuned by nature. It contains zootoxins and facilitates the subduing of prey and defence against threats. It is injected through unique fangs during a bite. It consists of enzymatic and non-enzymatic proteins and peptides, which are classified into different families based on their 파충류샵 function.
It is a natural gift
Snakes are endowed with a lethal secretion, called venom, that is fine-tuned by millions of years of evolution. This venom has numerous proteins and peptides that act with high selectivity and affinity on membrane receptors, ion channels, enzymes, and various hemostatic pathways . Animal venoms have long been the focus of research for their pharmacological activity and potential medical applications. They are an excellent source of bioactive molecules, and many snake venom components have been successfully isolated and characterized.
Studies show that the type of venom a snake has depends on its habitat and prey. Venom that acts quickly works well for small, fast-escaping prey such as fish, while venom that acts slowly is more effective against larger, slower-moving prey like mice. Snakes also produce multiple toxins, so that a single bite can cause different symptoms in different people.
Serine proteinases from the venom of a snake are also an important component of the toxic effect. These enzymes have a wide variety of actions that include anticoagulant, antimicrobial, platelet aggregation inhibitory, and apoptotic inducing activities. They are found mainly in the venom of Viperidae, Crotalidae, and Elapidae snakes and less frequently in the venom of Hydrophiidae snakes.
L-amino acid oxidases (LAAOs) are flavoenzymes that stimulate the stereospecific oxidative deamination of an L-amino acid to form an ammonia and a hydrogen peroxide. LAAOs are found mainly in the venoms of Viperidae and Crotalidae snakes, and they have many important biological activities to include anticoagulant, antimicrobial, and platelet aggregation inhibitory.
It is a weapon
Whether delivered through vipers, cobras, or kraits’ unique fangs or spitted by lizards, snake and lizard venom is one of nature’s deadliest innovations. Each year, these chemical weapons kill up to 200,000 humans and millions of rodents, birds, and other animals. But the deadly chemicals are also stirring a heated debate in academia about their evolutionary origins. Ostensibly, the squabble centers on whether venom evolved just once or on repeated occasions among different types of snakes and lizards. But it’s really about the see-sawing of scientific truth, and how some hypotheses become enshrined as facts.
Advances in molecular techniques have revealed the complex chemical composition of reptilian venoms. These methods, along with new advances in transcriptomics and proteomics, are revolutionizing the field of venomomics.
It is a defence mechanism
The venom of some snake species, including the spitting cobra, contains a variety of proteins and peptides that target the nervous system. These toxins, called cytotoxins, are injected by the snake’s unique fangs during bites or by spit. The venom has evolved as a defence mechanism to immobilize prey and deter predators. The venom is also rich in peptides that affect cell membrane receptors and ion channels, blocking or stimulating them. These toxins are grouped into a large number of protein families. Over millions of years of evolution, these toxins have become optimized to achieve long-term pharmacodynamic effects against specific molecular targets, such as coagulation cascade proteins, receptors, and ion channels.
The majority of snake venom components are non-enzymatic, and act on hemotoxic or neurotoxic targets. These include metalloproteinases, phosphatases, and fibrinolysins. The venom of the prairie rattlesnake, Crotalus viridis, includes metalloproteinases that help digest the snake’s prey. It also contains heparin-like peptides that can cause blood clots in the lungs. The venom of the Australian bandicoot, Boiga dendroaspis, has been shown to be toxic to birds.
Despite its complex composition, snake venom is relatively easy to isolate and analyse. Advances in transcriptomics, proteomics, and next-generation sequencing have enabled the study of thousands of venom components. This field of research is known as venomics and has revealed the chemical richness of snake venom. Generally, a single toxin has hundreds of isoforms. The venomics results show that most of the venom components are peptides, and most of them belong to one of 30 families.
It is a source of food
Venoms are complex mixtures of biological compounds that act primarily on ion channels and G-protein coupled membrane receptors. They are secreted from venom glands and delivered through spurs, stingers or fangs to kill or paralyze prey, and for self-defense. They are derived from a wide range of animals, including reptiles, amphibians, fishes, spiders, insects and jellyfish.
Snake venoms are composed of 20 to 100 components, with the majority consisting of peptides and proteins. They exhibit a variety of bioactivities, such as neurotoxicity, haemotoxicity and cytotoxicity. Moreover, venom composition can vary within a species due to various factors such as age, sex, and diet.
Venomics studies have recently revealed the complexity of snake venoms, with some protein families present in tens to hundreds of isoforms. Toxins from the PLA2, SVMP, and SVSP protein families are predominant in the venoms of most medically relevant snake species. The latter family contains several toxins that induce defibrinogenation, such as batroxobin (Defibrase), a thrombin-like serine protease from the Brazilian lancehead pit viper (Bothrops moojeni).
However, only a few snake venom peptides have been successfully developed into drugs. Despite this, the use of animal venoms in medicine continues to grow. While developing a drug from animal venoms is a time-consuming and risky process, the potential to treat a number of diseases makes it worthwhile.