Premathilaka, M. B. | bioRxiv Science

bioRxiv2026

Early Steps in Pathogen-induced TTR-amyloid-formation

Motivated by correlations between SARS-COV-2 infections and transthyretin (TTR) amyloidosis we use molecular dynamics simulations to study whether three protein fragments from the SARS-CoV-2 virus can initiate dissociation of the transthyretin (TTR) homotetramer as the first step on the pathway to TTR amyloidosis. We find that the peptides reduce the frequency of transient hydrogen bonds at the monomer-monomer interfaces, decreasing in this way the stability of the TTR tetramer.

molecular biology↗

bioRxiv2025

Modulation of Aβ1-42 Aggregation by a SARS-COV-2 Protein Fragment

A number of studies have pointed out to the possibility that SARS-COV-2 infections could trigger amyloid diseases such as Parkinsons disease or type-II diabetes. In the present study we probe this question for Alzheimers disease which is connected with presence of amyloids rich in A{beta}-peptides. For this purpose, we study by way of molecular dynamics simulations the interaction between the fragment FKNIDGYFKI of the Spike protein with A{beta}1-42 monomer and two fibril models, one patient-derived and one synthetic. Our results are compared with previous studies of other amyloid-forming proteins to identify commonalities and differences in the modulation of amyloid-formation by the viral protein fragment. Table of Contents Figure O_FIG O_LINKSMALLFIG WIDTH=200 HEIGHT=111 SRC="FIGDIR/small/669385v1_ufig1.gif" ALT="Figure 1"> View larger version (28K): org.highwire.dtl.DTLVardef@e9d5e7org.highwire.dtl.DTLVardef@1da47baorg.highwire.dtl.DTLVardef@19b1ad4org.highwire.dtl.DTLVardef@1fe5832_HPS_FORMAT_FIGEXP M_FIG C_FIG

molecular biology↗