Snake venom is an abundant resource of diverse pharmacologically bioactive proteins and peptides and a good natural source of
drug lead compounds and used as important research tools in the field of toxicology, pharmacology and neuroscience. Three
finger toxins (3FTx) is an important super-family of snake venom proteins which has a conserved three finger like appearance in
three dimensional structures. Members of 3FTx family show a wide array of pharmacological effects by targeting different
receptors and ion channels with high specificity and many of them are being investigated as potential drug target. Therefore, with
a vision to verdict a new edge and attempt we determined the amino acid compositional (%) profile, physiochemical properties,
secondary structural and functional analysis and phylogenetic relationship of three finger toxins present in four different elapid
snake species namely, Naja naja, Astrotia stokesii, Hydrophis cyanocintus and Pelamis platura using different bioinformatics tools. From
the outcome of the current studies, it will be possible to know about a range of biological functions which are responsible mainly
for the glowing amino acid composition profile of these proteins. Amino acid composition (%) profile although represents
differential amount of different amino acid residues which encompasses a family precise model but all the protein sequence have a
conserved amount of cysteine. The analysis of physicochemical properties can be used as a basic approach to contribute in
developing rational drug through protein engineering and understanding different physiological function which will be beneficial
for the welfare of human being.
Computational protein sequence analysis is one of the most important tools used for understanding the evolution of closely related proteins sequences including snake venom metalloproteinase sequences (SVMPs) which give valuable information regarding genetic variations. The fundamental objective of the present study is to screen the evolution distributed in metalloproteinase domain regions of protein sequences among different SVMPs in snake species which are involved in a range of pathological disorders such as arthritis, atherosclerosis, liver fibrosis, cardiovascular, cancer, liver and neurodegenerative disorders. In fact, SVMPS are responsible for hemorrhage and may also interfere with the hemostatic system. A comparative characterization of the metalloproteinase sequences has been carried out to analyze their multiple sequence alignment, phylogenic tree, homology, physicochemical, secondary structural and functional properties. DNAMAN software was used for multiple sequence alignment, phylogenic tree and homology and Expasy's Prot-param server was used for amino acid composition, physico-chemical and functional characterization of these SVMPs sequences. Studies of secondary structure of these SVMPs were carried out by computational program. Based on the observed patterns of occurrence of atypical features, we hypothesize that amino acids of metalloproteinase domain region (66.63% identity) of protein sequences are highly changeable; whereas, signal peptide region (93.98% identity) is the lowest changeable protein sequence and the remaining other three domains such as propeptide region (87.36% identity), desintegrin domain region (78.63% identity) and cysteine-rich domain region (75.70% identity) show moderate changeable protein sequence. SVMPs might be an accelerated evolution, which is a key player in causing diseases. From the data, it can be suggested that over -changed metalloproteinase domain regions in snake venom metalloproteinase might be responsible for the generation of functional variation of proteins expressed, which in turn may lead to different disorders in humans after snake bite. The results of this study would be an effective tool for the study of mutation, drugs resistance mechanisms and development of new drugs for different diseases.
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