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Research Article

Triazavirine supramolecular complexes as modifiers of the peptide oligomeric structure

ORCID Icon, ORCID Icon, & ORCID Icon
Pages 2694-2698 | Received 20 Jun 2017, Accepted 06 Aug 2017, Published online: 12 Sep 2017
 

Abstract

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.

Acknowledgements

The results of the work were obtained using computational resources of Department of Information and Computational Technologies of the St. Petersburg State Polytechnic University (http://www.spbstu.ru). We thanks Mr. Edward Ramsay for the help in writing the manuscript and Dr. D. V. Lebedev (DMRB PNPI NRC KI) for the fruitful discussion of the experiments.

Notes

No potential conflict of interest was reported by the authors.

The supplementary material for this article is available online at https://doi.org/10.1080/07391102.2017.1367329.

Additional information

Funding

This study was supported by the Russian Foundation for Basic Research, [project number 14-24-01103 ofi_m].

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