Journal
JOURNAL OF BIOMOLECULAR STRUCTURE & DYNAMICS
Volume 36, Issue 10, Pages 2694-2698Publisher
TAYLOR & FRANCIS INC
DOI: 10.1080/07391102.2017.1367329
Keywords
amyloid-like; triazavirine; ionic peptide; molecular dynamics; gromacs
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Funding
- Russian Foundation for Basic Research [14-24-01103 ofi_m]
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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.
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