bioRxivBiophysics
A double-edged sword: supramolecular complexes of triazavirine display multicenter binding effects which influence aggregate formation
Y. A. Zabrodskaya, A. V. Shvetsov, V. B. Tsvetkov, V. V. Egorov
Abstract
Triazavirine (TZV), a small molecule with a broad spectrum of antiviral activity, shows a tendency to induce the aggregation of melittin (MLT), a cationic membrane-disrupting peptide from the poison of the European bee. In MLT:TZV mixtures, high molecular weight precipitates form once a critical MLT:TZV ratio has been exceeded. Molecular dynamics simulation of MLT-TZV interactions, followed by molecular docking, led us to the hypothesis of multicenter binding of TZV supramolecular complexes to MLT.
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