Abstract
Snakes are equipped with their venomic armory to tackle different prey and predators in adverse natural world. The venomic composition of snakes is a mix of biologically active proteins and polypeptides. Among different components snake venom cytotoxins and short neurotoxin are non-enzymatic polypeptide candidates with in the venom. These two components structurally resembled to three-finger protein superfamily specific scaffold. Different non-toxin family members of three-finger protein superfamily are involved in different biological roles. In the present study we analyzed the snake venom cytotoxins, short neurotoxins and related non-toxin proteins of different chordates in terms of amino acid sequence level diversification profile, polarity profile of amino acid sequences, conserved pattern of amino acids and phylogenetic relationship of these toxin and nontoxin protein sequences. Sequence alignment analysis demonstrates the polarity specific molecular enrichment strategy for better system adaptivity. Occurrence of amino acid substitution is high in number in toxin sequences. In non-toxin body proteins there are less amino acid substitutions. With the help of conserved residues these proteins maintain the three-finger protein scaffold. Due to system specific adaptation toxin and non-toxin proteins exhibit a varied type of amino acid residue distribution in sequence stretch. Understanding of Natural invention scheme (recruitment of venom proteins from normal body proteins) may help us to develop futuristic engineered bio-molecules with remedial properties.
Highlights
In the domain of biology and biochemistry interpreting the evolutionary process of life is of great importance
Results & Discussion: In this work, various snake venom cytotoxins and short neurotoxins and related chordate specific non-toxin proteins were analyzed with the help of different bioinformatical packages to address evolutionary process of these molecules Table 1
First residue of all sequences is a Leu which is conserved in all peptides except in short neurotoxins, Secreted Ly-6/uPAR-related protein 1 (SLURP1) of human and Secreted Ly-6/uPAR-related protein 2 (SLURP2) of human
Summary
In the domain of biology and biochemistry interpreting the evolutionary process of life is of great importance. The journey of evolution assisted with natural selection generates improved biologically functional protein molecules [1]. The process of evolution gifted a precious thesaurus to the snakes, i.e., their venom. The primary function of snake venom is to incapacitation and immobilization of the prey of the snakes (as an offensive armory). The evolution of venoms favors the survival of snakes in different environment [3]. Snake venom is a cornucopia of biologically active polypeptides and non-polypeptide constituents [4]. Among the different venomic component snake venom cytotoxins and short neurotoxins are nonenzymatic polypeptide candidates with a molecular weight of 5-10 kDA [4]. Fifty percent of the dry weight accounts for its cytotoxin components [5]. The characteristics of cytotoxins and short neurotoxins are i) three
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