Abstract
The mechanism of conversion of the normal prion protein (PrPC) into aggregates of its pathological conformer (PrPSc) reamins unclear. The aim of this study was to evaluate the effects induced by exposure of biological samples containing PrPSC to a magnetic field induced prominent molecular changes of samples indicated by the IR spectra located in the region that contains contribution primarily from absorption of amides. This finding suggests the existence of a strong correlation between magnetism and PrPsc and supports a new hypothesis that explains the conversion of normal PrPc to abnormal isoform PrPsc.
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Schedule a callMore From: Journal of Biological Research - Bollettino della Società Italiana di Biologia Sperimentale
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