Nanoformulation of the Broad-Spectrum Hydrophobic Antiviral Vacuolar ATPase Inhibitor Diphyllin in Human Recombinant H-ferritin

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Date
2024-04-30
Authors
Vojníková, Michaela
Súkupová, Martina
Štefánik, Michal
Straková, Petra
Haviernik, Jan
Kapolková, Kateřina
Gruberová, Eliška
Rašková, Klára
Michálková, Hana
Švec, Pavel
Advisor
Referee
Mark
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Dove Press
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Abstract
As highlighted by recent pandemic outbreaks, antiviral drugs are crucial resources in the global battle against viral diseases. Unfortunately, most antiviral drugs are characterized by a plethora of side effects and low efficiency/poor bioavailability owing to their insolubility. This also applies to the arylnaphthalide lignin family member, diphyllin (Diph). Diph acts as a vacuolar ATPase inhibitor and has been previously identified as a promising candidate with broad-spectrum antiviral activity. However, its physicochemical properties preclude its efficient administration in vivo, complicating preclinical testing.
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Peer-reviewed
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Published version
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en
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Defence
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Creative Commons Attribution-NonCommercial 3.0 Unported
http://creativecommons.org/licenses/by-nc/3.0/
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