Chesney, A. D. | Search bioRxiv

bioRxiv2023

Human Amylin in the Presence of SARS-COV-2 Protein Fragments

Covid-19 can lead to the onset of type-II diabetes which is associated with aggregation of islet amyloid polypeptides, also called amylin. Using molecular dynamics simulations, we investigate how the equilibrium, between amylin monomers in its functional form and fibrils associated with diabetes, is altered in presence of SARS-COV-2 protein fragments. For this purpose, we study the interaction between the fragment SFYVYSRVK of the Envelope protein or the fragment FKNIDGYFKI of the Spike protein with the monomer and two amylin fibril models. Our results are compared with earlier work studying such interactions for two different proteins.

biophysics↗

bioRxiv2022

Effect of an amyloidogenic SARS-COV-2 protein fragment on α-synuclein monomers and fibrils

Using molecular dynamic simulations we study whether amyloidogenic regions in viral proteins can initiate and modulate formation of -synuclein aggregates, thought to be the disease-causing agent in Parkinsons Disease. As an example we choose the nine-residue fragment SFYVYSRVK (SK9), located on the C-terminal of the Envelope protein of SARS-COV-2. We probe how the presence of SK9 affects the conformational ensemble of -synuclein monomers and the stability of two resolved fibril polymorphs. We find that the viral protein fragment SK9 may alter -synuclein amyloid formation by shifting the ensemble toward aggregation-prone and preferentially rod-like fibril seeding conformations. However, SK9 has only little effect of the stability of pre-existing or newly-formed fibrils.

biophysics↗