International journal of pharmaceutics · 2025
Plasminogen-cyclodextrin aerosol for ARDS: activity retention in simulated oxygen therapy and inflammation-triggered clot lysis.
СтатьяНазвание и аннотация: Перевод пока не подготовлен
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Vizzoni Lucia, Migone Chiara, Nesti Siria Emily, Bona Nicolò Della, Franzini Maria, Brogi Simone, Calderone Vincenzo, Fabiano Angela, Zambito Ylenia, Mori Filippo, Ferro Baldassare, Piras Anna Maria
Аннотация
Acute Respiratory Distress Syndrome (ARDS) involves intense pulmonary inflammation, endothelial damage, and fibrin accumulation, often requiring oxygen therapy. Plasminogen (PLG), a fibrinolytic zymogen, has therapeutic potential for resolving fibrin deposits in the lungs but is vulnerable to oxidative degradation during aerosolization. This study presents a clinically feasible inhalable formulation of PLG complexed with hydroxypropyl-β-cyclodextrin (HP-β-CD), intended to preserve enzymatic function during nebulization under oxygen-rich conditions. Using a ready-to-use eye-drop solution (PLG-OMP), the formulation is repurposed for off-label inhalable administration and prepared with minimal handling suitable for hospital pharmacy protocols. Spectroscopic analyses confirmed complexation, and FT-IR demonstrated HP-β-CD's protective effect against methionine oxidation. Consistently, computer-based investigation at oxidation-relevant sites revealed binding of HP-β-CD close to methionine residues, supporting the spectroscopic evidence of a shielding effect. Aerodynamic evaluation via mesh nebulization showed favorable lung deposition profiles (MMAD ∼ 2.1 μm, FPF ∼ 84 %). Enzymatic activity post-nebulization in oxygen flow remained > 95 % when complexed with HP-β-CD, compared to ∼ 57 % for unprotected PLG. In vitro lysis of human clots was confirmed in both urokinase-triggered and cell-activated degradation models. The latter employed a cell-based model wherein LPS-stimulated macrophages-triggered lysis of human clots through inflammation-induced activation of nebulised PLG. D-dimer quantification verified consistent fibrinolytic performance across both models. These results establish a robust foundation for targeted fibrinolytic therapy in ARDS, combining formulation simplicity with biological relevance to support clinical translation.