Analysis of electronic structure of human abnormal prion protein which form amyloid fibrils and its normal prion protein

Abstract

Prions disease are fatal neurodegenerative diseases caused by abnormal prion protein aggregate. In prion proteins that have the same primary structure, the cause of the structural change from the normal form to the abnormal form is still unknown. In this study, canonical molecular orbital （CMO） calculations of normal and abnormal prions were carried out. The results showed that the electronic structure of the normal and abnormal forms is significantly different and normal prion was more stable than abnormal prion in a single structure. Estimating interaction energies of layer formation from CMO calculation suggested that abnormal prions were stable with layer structure, and amyloid fibril formation was accelerated.