Author(s)

Laura Alejandra Mandujano-Rosas¹, Daniel Osorio-González^1*, Pedro Guillermo Reyes-Romero², Jorge Mulia-Rodríguez¹

¹Laboratory of Molecular Biophysics, Faculty of Sciences, Autonomous University of State of Mexico, Toluca, Mexico.
²Laboratory of Advaced Physics, Faculty of Sciences, Autonomous University of State of Mexico, Toluca, Mexico.

Prion proteins are related to the development of incurable and invariably fatal neurodegenerative diseases in humans and animals. The pathogenicity involves the conversion of the host-encoded-alpha rich isoform of prion protein, PrP^C, into a misfolded beta-strand rich conformer, PrP^Sc. Although it has already been described that many punctual mutations alter the stability of PrP^C, making it more prone to adopt an abnormal misfolded structure, the majority of cases reported among general population are sporadic in wild-type organisms. Thus, in this work we studied the dynamics and stability profiles of wild-type human prion protein by Molecular Dynamics (MD) simulation at different solvent temperatures. This analysis brought out certain residues and segments of the prion protein as critical to conformational changes; these results are consistent with experimental reports showing that protein mutants in those positions are related to the development of disease.

Prion Protein, Misfolding Susceptibility, Molecular Dynamics Simulation

Mandujano-Rosas, L. , Osorio-González, D. , Reyes-Romero, P. and Mulia-Rodríguez, J. (2014) Human Prion Protein Conformational Changes Susceptibility: A Molecular Dynamics Simulation Study. Open Journal of Biophysics, 4, 169-175. doi: 10.4236/ojbiphy.2014.44016.