Molecular dynamics simulations of amyloid Aß structures

The existence of Aβ40 and Aβ42, their aggregates, and their interaction are some pathological characteristics of Alzheimer's disease. Numerous clinical case studies throughout the COVID-19 pandemic revealed that the SARS-COV-2 causes aggravate the course of Alzheimer's disease and upsurge mortality rates. The investigation element of our study is to probe how the stability of the homogeneous (Aβ40) fibril model and 1:1 cross-seeded Aβ40 and Aβ42 fibrils of the heterogeneous (Aβ40/Aβ42) fibril model are impressed by the presence of the amyloidogenic Ser55PheTyrValTyrSerArgValLys63 (SK9) peptide of the SARS-COV-2 E-protein (envelope protein). Our analysis demonstrated that there are no prominent dissimilarities between the stability of the heterogeneous and the homogeneous fibril model. However, we observed the central hydrophobic region of the heterogeneous fibril model interacts more with the residues of the carboxyl-terminal hydrophobic region (unpublished data).