J 2024

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

VOJNIKOVA, Michaela; Martina SÚKUPOVÁ; Michal STEFANIK; Petra STRAKOVÁ; Jan HAVIERNIK et al.

Základní údaje

Originální název

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

Autoři

VOJNIKOVA, Michaela; Martina SÚKUPOVÁ; Michal STEFANIK; Petra STRAKOVÁ; Jan HAVIERNIK; Katerina KAPOLKOVA; Eliska GRUBEROVA; Klara RASKOVA; Hana MICHALKOVA; Pavel SVEC; Marie PESKOVA KUDLICKOVA; Ivana HUVAROVA; Daniel RŮŽEK; Jiří SALÁT; Vladimir PEKARIK; Luděk EYER a Zbyněk HEGER

Vydání

International Journal of Nanomedicine, Dove Medical Press Ltd, 2024, 1178-2013

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10607 Virology

Stát vydavatele

Nový Zéland

Utajení

není předmětem státního či obchodního tajemství

Odkazy

Impakt faktor

Impact factor: 6.500

Označené pro přenos do RIV

Ano

Kód RIV

RIV/00216224:14310/24:00138757

Organizační jednotka

Přírodovědecká fakulta

EID Scopus

Klíčová slova anglicky

drug delivery; SARS-CoV-2; TBEV; WNV; Zika virus

Štítky

Příznaky

Mezinárodní význam, Recenzováno
Změněno: 17. 3. 2025 14:53, Mgr. Marie Novosadová Šípková, DiS.

Anotace

V originále

Background: 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. Methods: We produced human recombinant H-ferritin (HsaFtH) and used it as a delivery vehicle for Diph encapsulation through pH-mediated reversible reassembly of HsaFtH. Diph nanoformulation was subsequently thoroughly characterized and tested for its non-target cytotoxicity and antiviral efficiency using a panel of pathogenic viral strain. Results: We revealed that loading into HsaFtH decreased the undesired cytotoxicity of Diph in mammalian host cells. We also confirmed that encapsulated Diph exhibited slightly lower antiviral activity than free Diph, which may be due to the differential uptake mechanism and kinetics of free Diph and Diph@HsaFtH. Furthermore, we confirmed that the antiviral effect was mediated solely by Diph with no contribution from HsaFtH. Conclusion: It was confirmed that HsaFtH is a suitable vehicle that allows easy loading of Diph and production of highly homogeneous nanoparticles dispersion with promising broad-spectrum antiviral activity.