Evolution of camel CYP2E1 and its associated power of binding toxic industrial chemicals and drugs |
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| Affiliation: | 1. Department of Physiology, Biochemistry and Pharmacology, Faculty of Veterinary, King Faisal University, Alhofuf, Alahsa, Saudi Arabia;2. Department of Pharmacology, Faculty of Veterinary Medicine, Kafrelshikh University, Kafrelshikh 33516, Egypt,;3. Department of Chemistry and Biomolecular Science, Faculty of Engineering, Gifu University, Japan;4. Department of Applied Chemistry, Faculty of Engineering, Aichi Institute of Technology, Yachigusa 1247, Yakuza, Toyota 470-0392, Japan;1. Department of Pharmacology, Faculty of Medicine and Dentistry, Palacky University, Hnevotinska 3, 775 15 Olomouc, Czech Republic;2. Department of Medical Chemistry and Biochemistry, Faculty of Medicine and Dentistry, Palacky University, Hnevotinska 3, 775 15 Olomouc, Czech Republic;3. Department of Toxicology and Military Pharmacy, Faculty of Military Health Sciences, University of Defense, 500 01 Hradec Kralove, Czech Republic;4. Biomedical Research Center, University Hospital Hradec Kralove, 500 01 Hradec Kralove, Czech Republic;1. University of Patras, Department of Chemical Engineering, University Campus, 26500 Patras, Greece;2. Institute of Chemical Engineering Sciences, Stadiou Str., Platani, P.O. Box 1414, GR-26500 Patras, Greece;1. School of Traditional Chinese Materia Medica, Shenyang Pharmaceutical University, Shenyang 110016, China;2. School of Life Science and Biological Pharmacy, Shenyang Pharmaceutical University, Shenyang 110016, China;1. Department of Pharmacology and Toxicology, Faculty of Pharmacy in Hradec Kralove, Charles University in Prague, Heyrovskeho 1203, Hradec Kralove, CZ-500 05, Czech Republic;2. Department of Cell Biology and Genetics, Faculty of Science, Palacky University in Olomouc, Slechtitelu 11, Olomouc, CZ-783 71, Czech Republic;3. Unidad Mixta Hepatología Experimental, Hospital La Fe & University of Valencia (Dep. Biochemistry and Molecular Biology), Av. Campanar, 21, 46009 Valencia, Spain;4. CIBERehd, Centro de Investigación Biomédica en Red de Enfermedades Hepáticas y Digestivas, Barcelona, Spain |
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| Abstract: | 
Camels are raised in harsh desert environment for hundreds of years ago. By modernization of live and the growing industrial revolution in camels rearing areas, camels are exposed to considerable amount of chemicals, industrial waste, environmental pollutions and drugs. Furthermore, camels have unique gene evolution of some genes to withstand living in harsh environments. In this work, the camel cytochrome P450 2E1 (CYP2E1) is compromised to detect its evolution rate and its power to bind with various chemicals, protoxins, procarcinogens, industrial toxins and drugs. In comparison with human CYP2E1, camel CYP2E1 more efficiently binds to small toxins as aniline, benzene, catechol, amides, butadiene, toluene and acrylamide. Larger compounds were more preferentially bound to the human CYP2E1 in comparison with camel CYP2E1. The binding of inhalant anesthetics was almost similar in both camel and human CYP2E1 coinciding with similar anesthetic effect as well as toxicity profiles. Furthermore, evolutionary analysis indicated the high evolution rate of camel CYP2E1 in comparison with human, farm and companion animals. The evolution rate of camel CYP2E1 was among the highest evolution rate in a subset of 57 different organisms. These results indicate rapid evolution and potent toxin binding power of camel CYP2E1. |
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| Keywords: | Cytochrome P450 Docking Evolution rate Binding Molecular modeling |
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