TY - JOUR T1 - Triazavirine supramolecular complexes as modifiers of the peptide oligomeric structure JF - bioRxiv DO - 10.1101/150664 SP - 150664 AU - Alexey V. Shvetsov AU - Yana A. Zabrodskaya AU - Peter A. Nekrasov AU - Vladimir V. Egorov Y1 - 2017/01/01 UR - http://biorxiv.org/content/early/2017/06/16/150664.abstract N2 - 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. ER -