Silver nanoparticles (AgNPs) are excellent antimicrobial agents and promising candidates for preventing or treating bacterial infections caused by antibiotic resistant strains. However, their increasing use in commercial products raises concerns about their environmental impact. In addition, traditional physicochemical approaches often involve harmful agents and excessive energy consumption, resulting in AgNPs with short-term colloidal stability and silver ion leaching. To address these issues, we designed stable hybrid lignin-silver nanoparticles (AgLigNPs) intended to effectively hit bacterial envelopes as a main antimicrobial target. The lignin nanoparticles (LigNPs), serving as a reducing and stabilizing agent for AgNPs, have a median size of 256 nm and a circularity of 0.985. These LigNPs were prepared using the dialysis solvent exchange method, producing spherical particles stable under alkaline conditions and featuring reducing groups oriented toward a wrinkled surface, facilitating AgNPs synthesis and attachment. Maximum accumulation of silver on the LigNP surface was observed at a mass reaction ratio mAg:mLig of 0.25, at pH 11. The AgLigNPs completely inhibited suspension growth and reduced biofilm development by 50% in three tested strains of Pseudomonas aeruginosa at a concentration of 80/9.5 (lignin/silver) mg L-1. Compared to unattached AgNPs, AgLigNPs required two to eight times lower silver concentrations to achieve complete inhibition. Additionally, our silver-containing nanosystems were effective against bacteria at safe concentrations in HEK-293 and HaCaT tissue cultures. Stability experiments revealed that the nanosystems tend to aggregate in media used for bacterial cell cultures but remain stable in media used for tissue cultures. In all tested media, the nanoparticles retained their integrity, and the presence of lignin facilitated the prevention of silver ions from leaching. Overall, our data demonstrate the suitability of AgLigNPs for further valorization in the biomedical sector.

• Publication type
• Journal Article MeSH

Fullerene derivatives with hydrophilic substituents have been shown to exhibit a range of biological activities, including antiviral ones. For a long time, the anti-HIV activity of fullerene derivatives was believed to be due to their binding into the hydrophobic pocket of HIV-1 protease, thereby blocking its activity. Recent work, however, brought new evidence of a novel, protease-independent mechanism of fullerene derivatives' action. We studied in more detail the mechanism of the anti-HIV-1 activity of N,N-dimethyl[70]fulleropyrrolidinium iodide fullerene derivatives. By using a combination of in vitro and cell-based approaches, we showed that these C70 derivatives inhibited neither HIV-1 protease nor HIV-1 maturation. Instead, our data indicate effects of fullerene C70 derivatives on viral genomic RNA packaging and HIV-1 cDNA synthesis during reverse transcription-without impairing reverse transcriptase activity though. Molecularly, this could be explained by a strong binding affinity of these fullerene derivatives to HIV-1 nucleocapsid domain, preventing its proper interaction with viral genomic RNA, thereby blocking reverse transcription and HIV-1 infectivity. Moreover, the fullerene derivatives' oxidative activity and fluorescence quenching, which could be one of the reasons for the inconsistency among reported anti-HIV-1 mechanisms, are discussed herein.

• Keywords
• HIV-1, RNA packaging, fullerene, inhibition, nucleocapsid,
• MeSH
• Fullerenes metabolism   pharmacology   MeSH
• Genome, Viral drug effects   MeSH
• gag Gene Products, Human Immunodeficiency Virus metabolism   MeSH
• HEK293 Cells MeSH
• HIV-1 drug effects   genetics   metabolism   physiology   MeSH
• Anti-HIV Agents metabolism   pharmacology   MeSH
• Humans MeSH
• Nucleocapsid Proteins metabolism   MeSH
• Reverse Transcription MeSH
• RNA, Viral metabolism   MeSH
• Virus Uncoating drug effects   MeSH
• Protein Binding MeSH
• Virion metabolism   MeSH
• Viral Genome Packaging drug effects   MeSH
• Check Tag
• Humans MeSH
• Publication type
• Journal Article MeSH
• Research Support, Non-U.S. Gov't MeSH
• Names of Substances
• Fullerenes MeSH
• gag Gene Products, Human Immunodeficiency Virus MeSH
• Anti-HIV Agents MeSH
• Nucleocapsid Proteins MeSH
• RNA, Viral MeSH