Volume 8, Issue 3 (2022)                   Pharm Biomed Res 2022, 8(3): 199-204 | Back to browse issues page

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Jalali A, Mahdavinia M, Galehdari H, Baradaran M, Valdi-Biranvand D, Naderi Soorki M. Molecular Characterization of a cDNA Encoding of an Anionic Cysteine-Free Antimicrobial Peptide From the Iranian Scorpion Odontobuthus Doriae Venom Glands. Pharm Biomed Res 2022; 8 (3) :199-204
URL: http://pbr.mazums.ac.ir/article-1-452-en.html
Molecular Characterization of a cDNA Encoding of an Anionic Cysteine-Free Antimicrobial Peptide From the Iranian Scorpion Odontobuthus Doriae Venom Glands
Amir Jalali1 , Masoud Mahdavinia2 , Hamid Galehdari3 , Masoumeh Baradaran4 , Davood Valdi-Biranvand4 , Maryam Naderi Soorki * 3
1- Department of Operating Room, Langroud School of Allied Medical Sciences, Guilan University of Medical Sciences, Rasht, Iran.
2- Department of Toxicology, School of Pharmacy, Toxicology Research Center, Medical Basic Sciences Research Institute, Ahvaz Jundishapur University of Medical Sciences, Ahvaz, Iran.
3- Department of Biology, Faculty of Science, Shahid Chamran University of Ahvaz, Ahvaz, Iran.
4- Department of Toxicology, School of Pharmacy, Toxicology Research center, Medical Basic Sciences Research Institute, Ahvaz Jundishapur University of Medical Sciences, Ahvaz, Iran
Abstract:   (1089 Views)
Background: The venom peptides from the scorpion fauna of Iran have been poorly characterized so far.
Objectives: In this study, we identified a cDNA encoding of an anionic cysteine-free antimicrobial peptide from the Iranian yellow scorpion odontobuthus doriae (O.doriae).
Methods: The cDNA sequence of an anionic antimicrobial-peptide (AMP) was determined from the venom gland cDNA library of Iranian yellow scorpion O.doriae and was named ODAMP5. This sequence was characterized by a software. Then, the structure and function of its putative peptide were predicted in a bioinformatics manner. The library was constructed from 6 scorpion venom glands. The cDNA related to ODAMP5 was isolated from one positive clone of the library.
Results: The analysis of ODAMP5 reveals a 51-residue mature peptide with an anionic property that was stable in physiological states. ODAMP5 was similar to anionic peptide Aba-2 from Androctonus bicolor and according to its structure, it can be a member of helical structure AMPs with a new type of putative conserved domain. Putative ODAMP5 has a small size which makes it convenient for synthesis.
Conclusion: Furthermore, we created a framework to express the ODAMP5 peptide for future biomedical and pharmacological studies. ODAMP5 may be a new suitable therapeutic strategy for bacterial infection among a few recognized scorpion venom peptides without disulfide bridges.
Keywords: Anionic cysteine-free, Molecular characterization, cDNA library, Odontobuthus doriae, Venom glands
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Type of Study: Original Research | Subject: Biotechnology
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