Abstract
Nature endowed snakes with a lethal secretion known as venom, which has been fine-tuned over millions of years of evolution. Snakes utilize venom to subdue their prey and to survive in their natural habitat. Venom is known to be a very poisonous mixture, consisting of a variety of molecules, such as carbohydrates, nucleosides, amino acids, lipids, proteins and peptides. Proteins and peptides are the major constituents of the dry weight of snake venoms and are of main interest for scientific investigations as well as for various pharmacological applications. Snake venoms contain enzymatic and non-enzymatic proteins and peptides, which are grouped into different families based on their structure and function. Members of a single family display significant similarities in their primary, secondary and tertiary structures, but in many cases have distinct pharmacological functions and different bioactivities. The functional specificity of peptides belonging to the same family can be attributed to subtle variations in their amino acid sequences. Currently, complementary tools and techniques are utilized to isolate and characterize the peptides, and study their potential applications as molecular probes, and possible templates for drug discovery and design investigations.
Highlights
Nature has always been an intriguing source for drug design investigations
Disintegrins are cysteine-rich peptides that result from the post-translational cleavage of snake venom metalloproteases (SVMPs), which are phylogenetically related with ADAMS
Snake venom peptides have been identified to be mostly very stable, as they have to reach the site of action before the internal mechanisms of their prey degrades, neutralizes or excretes them
Summary
Nature has always been an intriguing source for drug design investigations. From among the animal kingdom, insects and reptilians are interesting and valuable sources for identifying molecules with potential pharmaceutical applications [1]. Various bioactive proteins and peptides have been reported from the venom of different species of snakes, conus, scorpions, centipedes, lizards, spiders, sea anemones, bees and octopus [1,2,3,4,5,6,7,8,9]. Snake venom which snakes useuse to immobilize andand digest theirtheir prey.prey It is used as a defensive and a survival tool [13]. We focus our discussion on snake venom peptides, theirtheir classification and and bioactivities. We define snake venom peptides as the group of non-enzymatic polypeptides in the venom which fold into monomeric domains and are smaller than. Snake venom toxins have proved to be invaluable tools in determining the structure and functions of receptors.
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