Strategic Nanoarchitectonics of Porous Beads for Protein-Bound Toxin Removal with Self-Photodecomposition and Visual Monitoring for Hyperbilirubinemia

Separating toxins from albumin is significantly more challenging than simply adsorbing the toxin/protein complex during blood purification. Bilirubin is distinctive among protein-bound toxins because its photodecomposition products are hydrophilic and readily dissociate from albumin. Inspired by phototherapy for neonatal jaundice, an innovative multifunctional adsorbent is proposed and equipped with self-photodecomposition and visual monitoring abilities. Herein, inverse opal beads (IOBs) is developed through strategic nanoarchitectonics. The periodic ordered structure of the IOBs imparts a self-hosted blue light emission property that facilitates the bilirubin photodecomposition. Additionally, the interconnected pores of the IOBs enhance the adsorption of bilirubin photodecomposition products. Moreover, the colors of the IOBs change in response to the amount of adsorbed bilirubin photodecomposition products, allowing for real-time visual monitoring of the adsorption state during hemoperfusion. These features allow the IOBs to effectively compete with albumin for toxin binding. In hyperbilirubinemia rats, the total bilirubin (TBIL) clearance ratios achieved by the IOBs and a commercial adsorbent (BS330) are 45.1% and 29.3%, respectively. Notably, albumin (ALB) concentration decreased by 31.8% after treatment with BS330, whereas no significant change is observed in the IOB-treated group. These results suggest that IOBs hold great potential as a highly promising adsorbent for treating hyperbilirubinemia.
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