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.
Snake venom contains a diverse array of pharmacologically active proteins and polypeptides that have led to the development of molecular probes and therapeutic agents. Short neurotoxins and cytotoxins are non-enzymatic polypeptides components of snake venom found only in the venoms of Elapidae (cobras, kraits, mambas, coral snakes and Australian elapids) and Hydrophidae (sea snakes). The three-dimensional structure of short neurotoxins and cytotoxins has three beta stranded loops resembling three-fingers of three-finger protein super family. This protein super family has different family members which are employed in various biological functions. The objective of this study is to search out the amino acid compositional (%) profile, physiochemical properties and functional analysis of three finger toxins present in different elapid snake species to be precise, Bungarus fasciatus, Naja naja and Naja kauthia. We analyzed a total of 23 reference protein sequences representing short neurotoxin and cytotoxin of three elapid snakes and related non-toxin proteins of human in terms of functional analysis, amino acid compositional (%) profile, number of amino acids, molecular weight, theoretical isoelectric point (pI), number of positively charged and negatively charged amino acid residues, instability index and grand average of hydropathy using computational tools. From the result it was found that amino acid composition profile represents that all sequences hold a conserved cysteine amount even as differential amount of different amino acid residues have a particular family pattern. It will also assist to know about involvement in various biological functions those are accountable for the vivid amino acid composition profile of these proteins. This comparative analysis of physicochemical properties would play a significant role in understanding the mechanisms of action of toxins and in the development of lead therapeutic molecules.
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