Abstract <p><i>In situ</i> forming hydrogels catalyzed by peroxidase systems hold promise for injectable and minimally invasive biomedical applications. We developed a biomimetic catalytic platform by multi-functionalizing hemin with gelatin and histamine (Ge–His–He) to enhance horseradish peroxidase (HRP)-like activity and enable controlled hydrogelation. The conjugate was synthesized through EDC/NHS coupling of gelatin and histamine, followed by coordination of the histamine imidazole with the Fe(III) center of hemin. Spectroscopic analyses confirmed amide formation and Fe–N coordination, validating successful integration. Kinetic studies with guaiacol and pyrogallol revealed superior catalytic efficiency and oxidative stability compared to free hemin, maintaining activity under high H<sub>2</sub>O<sub>2</sub> where HRP is deactivated. Cytocompatibility assays showed over 90% fibroblast viability, indicating low cytotoxicity. Ge–His–He effectively catalyzed Gel–Tyr crosslinking into hydrogels with tunable gelation time and porous microstructures. This stable, biocompatible HRP mimetic provides a promising enzyme-free approach for <i>in</i><i> situ</i> hydrogelation in various biomedical applications.</p> Graphical abstract <p></p>

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Multi-functionalization of hemin with gelatin and histamine to enhance the horseradish peroxidase catalytic activities for in situ hydrogelation

  • Phuong Le Thi,
  • Van Du Cao,
  • Anh Quan Hoang,
  • Dinh Trung Nguyen,
  • Quang Anh Tu,
  • Dinh-Chuong Pham,
  • Ngoc Quyen Tran,
  • Van Toan Nguyen

摘要

Abstract

In situ forming hydrogels catalyzed by peroxidase systems hold promise for injectable and minimally invasive biomedical applications. We developed a biomimetic catalytic platform by multi-functionalizing hemin with gelatin and histamine (Ge–His–He) to enhance horseradish peroxidase (HRP)-like activity and enable controlled hydrogelation. The conjugate was synthesized through EDC/NHS coupling of gelatin and histamine, followed by coordination of the histamine imidazole with the Fe(III) center of hemin. Spectroscopic analyses confirmed amide formation and Fe–N coordination, validating successful integration. Kinetic studies with guaiacol and pyrogallol revealed superior catalytic efficiency and oxidative stability compared to free hemin, maintaining activity under high H2O2 where HRP is deactivated. Cytocompatibility assays showed over 90% fibroblast viability, indicating low cytotoxicity. Ge–His–He effectively catalyzed Gel–Tyr crosslinking into hydrogels with tunable gelation time and porous microstructures. This stable, biocompatible HRP mimetic provides a promising enzyme-free approach for in situ hydrogelation in various biomedical applications.

Graphical abstract