Protein-mediated stabilization of amphotericin B increases its efficacy against diverse fungal pathogens.

ABSTRACT: Amphotericin B (AMB), a potent and broad-spectrum antifungal agent, faces solubility and toxicity challenges in clinical use. In this study, we explored the ability of DewY and EAS_Δ15, class I fungal hydrophobin proteins with unique amphipathic properties and self-assembly capabilities, to stabilize AMB in solution. UV-visible spectroscopy confirmed the ability of hydrophobin proteins to stabilize the monomeric state of AMB in aqueous solution for up to 48 h. Further assays revealed that this effect was not exclusive to hydrophobins, however, as non-hydrophobin proteins provided similar stabilizing effects. AMB-protein combinations exhibited enhanced efficacy against diverse clinically relevant fungal pathogens, with 4- to 32-fold reductions in the effective in vitro dosa

SUBMITTER: Fernandes KE 

PROVIDER: S-EPMC12131825 | biostudies-literature | 2025 Jun

REPOSITORIES: biostudies-literature