ABSTRACT
Given the current context of the SARS-CoV-19 pandemic, among the interfering risky factors with the Aß peptide aggregation in the brains of Alzheimer's disease (AD) patients can be hyperpyrexia and increased intracranial pressure (ICP). According to our hypothesis on the relationship between hyperpyrexia and cognitive decline in AD, two models of Aß peptides were used in this study: the structure of AD amyloid beta-peptide and near-atomic resolution fibril structures of the Aß peptide. Therefore, the binding templates were constructed for Aß peptide regions able to bind 9 different metal ions. The fragment transformation method was used for the structural comparison between Aß chains. Molecular dynamics simulation (MDS) was applied using the Nose-Poincare-Anderson equation to generate a theoretically correct NPT (isothermal-isobaric ensemble). The smallest dissimilarities were observed in the case of Cu+ binding potential followed by Co2+, both with similar variation. Structural changes have also occurred as a result of the dynamic simulation. All these changes suggest an aggravating factor in both hyperpyretic and AD conditions. Our findings suggest that elevated temperature and increased intracranial pressure rise the effect of peptide aggregation, by converting α-helix motif to ß-sheet and random coil conformation, which are related to the formation of senile plaques in AD brains.