PreprintCC BY-NC-NDbioRxiv
Early Steps in Pathogen-induced TTR-amyloid-formation
- 1University of Oklahoma
Abstract
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.
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BibTeX
@misc{premathilaka2026early,
title = {{Early Steps in Pathogen-induced TTR-amyloid-formation}},
author = {M. B. Premathilaka and U. H. E. Hansmann},
howpublished = {bioRxiv},
year = {2026},
month = sep,
doi = {10.64898/2026.09.21.753243},
url = {https://www.biorxiv.org/content/10.64898/2026.09.21.753243v1},
note = {CC BY-NC-ND},
}
RIS
TY - UNPB
TI - Early Steps in Pathogen-induced TTR-amyloid-formation
AU - M. B. Premathilaka
AU - U. H. E. Hansmann
PY - 2026
DA - 2026/09/21
PB - bioRxiv
DO - 10.64898/2026.09.21.753243
UR - https://www.biorxiv.org/content/10.64898/2026.09.21.753243v1
AB - 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.
ER -