RT Journal Article
SR Electronic
T1 Triazavirine supramolecular complexes as modifiers of the peptide oligomeric structure
JF bioRxiv
FD Cold Spring Harbor Laboratory
SP 150664
DO 10.1101/150664
A1 Alexey V. Shvetsov
A1 Yana A. Zabrodskaya
A1 Peter A. Nekrasov
A1 Vladimir V. Egorov
YR 2017
UL http://biorxiv.org/content/early/2017/06/16/150664.abstract
AB In this study we present molecular dynamics simulations of the antiviral drug triazavirine, that affects formation of amyloid-like fibrils of the model peptide (SI). According to our simulations, triazavirine is able to form linear supramolecular structures which can act as shields and prevent interactions between SI monomers. This model, as validated by simulations, provides an adequate explanation of triazavirine’s mechanism of action as it pertains to SI peptide fibril formation.