مقالات پذیرفته شده در هفتمین کنگره بین المللی زیست پزشکی
A scorpion-derived alpha toxin: characterization and homology modelling
A scorpion-derived alpha toxin: characterization and homology modelling
Masoumeh Baradaran,1,*
1. Toxicology Research Center, Medical Basic Sciences Research Institute, Ahvaz Jundishapur University of Medical Sciences, Ahvaz, Iran
Introduction: Scorpion venom likes a treasure because of having medically important components. Venom of scorpion consists of a mixture of peptides and proteins, some of them are toxic. Ion channel modifiers are the most important of them. Some drugs have designed based on the snake and scorpion venoms. So, identification and characterization of venom compounds can be a useful path for drug discovery.
Methods: Here, analysis of transcriptome obtained from the venom gland of M. eupeus using total RNA extraction and cDNA library synthesis; revealed the presence of some toxin transcripts. Blasting the transcriptome against proteins databases, including NCBI and Uniprot was done to find alpha toxin(s). Physico-chemical properties one determined alpha toxin was calculated using bioinformatics software. Finally, Three-dimensional structure of this protein was determined by means of homology modelling.
Results: According to the blast we found a sodium channel blocker, alpha toxin in the venom of M. eupeus, named meuNaTx-2 and deposited in the Gene bank. The mature peptide of meuNaTx-2 has 66 AA. A molecular weight of, 7482g/MOL and a theoretical pI of 8.12 were estimated for it. Secondary structure analysis determined a Toxin-3 superfamily domain in the structure of this protein. meuNaTx-2 has eight cysteine residues, which forms four disulphide bridges contributed in a conserved cysteine-stabilized alpha/beta domain. The three-dimensional structure of meuNaTx-2 consists of one alpha-helix and two beta-sheets, each of them contains two beta-strands.
Conclusion: Analysis of transcriptome of M. eupeus venom glands identified an alpha toxin which potentially modify sodium channels. Characterization and structure of this protein showed that it can be a great candidate for more research. Herein reported information about this protein can lead us to further investigation about function or probably using in drug design.