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Int J Biol Macromol ; 177: 360-369, 2021 Apr 30.
Artigo em Inglês | MEDLINE | ID: mdl-33631259

RESUMO

Hematin has been used as an alternative enzyme catalyst to horseradish peroxidase (HRP) due to its iron-containing activity center. Although hematin and it derivatives have been widely used for polymerization of phenol/analine compounds, it has some drawbacks such as the limited solubility and reaction only at high pH condition. Herein, we report a nanosized biomimetic catalyst, hematin-decorated polyamidoamine dendrimer (G3.0-He) that can effectively catalyze the in situ hydrogelation of phenol-conjugated polymers under neutral pH condition. We demonstrate that G3.0-He particles are smaller than 100 nm and have excellent enzyme-mimetic functions. Interestingly, the nanosized catalyst is not inactivated at high H2O2 concentration. Compared to pure hematin, G3.0-He has significantly higher dispersion in acidic and neutral media, and preserves the percentage of survival of fibroblasts over 90%. Notably, G3.0-He possesses an exquisite HRP-mimicking activity in gelation of gelatin derivative with phenolic hydroxyl (tyamine) moieties under mild physiological conditions. The in vitro study demonstrated that Gel-Tyr hydrogel by G3.0-He catalyzed reaction had excellent cytocompatibility and an excellent scaffold for adhesion to fibroblast cells. Therefore, the designed minimalistic G3.0-He catalyst could serve as an effective catalytic alternative for HRP enzyme in the preparation of biomedical hydrogels.


Assuntos
Materiais Biomiméticos , Dendrímeros , Fibroblastos/metabolismo , Hemina , Teste de Materiais , Nanopartículas/química , Materiais Biomiméticos/química , Materiais Biomiméticos/farmacologia , Linhagem Celular , Dendrímeros/química , Dendrímeros/farmacologia , Hemina/química , Hemina/farmacologia , Peroxidase do Rábano Silvestre/química , Peroxidase do Rábano Silvestre/farmacologia , Humanos
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