Prion diseases are fatal neurodegenerative transmissible disorders characterized by accelerated conversion of cellular prion into misfolded isoform and its deposition in nervous tissues. Understanding the conversion mechanism is fundamental bases for developing a therapeutic strategy for these diseases. The main objective was to study probable synergistic effects of temperatures and calcium ions as suspected inducers of prion disease. In this work, using molecular dynamic method we simulated two sets of prion protein systems each at three temperatures, 30, 37 and 40°C, in the presence and absence of 0.1mM calcium ions. Our results indicated apparent synergistic effect between low temperature and 0.1mM concentration of calcium ions. Our findings provides clear interpretation for the prevalence of Bovine Spongiform Encephalopathy (BSE) between 1986 to 1993, during which meat and bone powders (with high concentration of calcium ions) were incorporated into cattle feeding regime and particularly the disease picks during the cold season of the year .
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Author Name: Mohammad Reza Dayer, Mohammad Saaid Dayer, Reza Golabgir Zadeh,Mahboubeh Baheri
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Keywords: Calcium ions, Prion Protein, Synergistic Effects, Misfolding, Molceular Dynamic simulation.
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EISSN: 2249 –1929
EOI/DOI: nill
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