1. Encapsulation of collagenase within biomimetically mineralized metal–organic frameworks: designing biocomposites to prevent collagen degradation
- Author
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Ana K. Bedran-Russo, Ana Flávia Sanches Borges, Odair Bim Júnior, Regina Célia Galvão Frem, Valdecir Farias Ximenes, Jader Barbosa Silva Flor, and Paulo Noronha Lisboa-Filho
- Subjects
chemistry.chemical_classification ,Proteases ,Biocompatibility ,Biomolecule ,02 engineering and technology ,General Chemistry ,Microporous material ,010402 general chemistry ,021001 nanoscience & nanotechnology ,01 natural sciences ,Mineralization (biology) ,Catalysis ,0104 chemical sciences ,chemistry.chemical_compound ,chemistry ,Chemical engineering ,COLÁGENO ,Imidazolate ,Materials Chemistry ,Collagenase ,medicine ,Metal-organic framework ,0210 nano-technology ,medicine.drug - Abstract
A growing class of multifunctional porous materials termed metal–organic frameworks (MOFs) has attracted attention for immobilization of biomolecules via self-assembly of inorganic and organic building blocks. Herein, we report the rapid formation of MOF shells surrounding collagen-degrading enzymes by using a biomimetic mineralization approach. Bacterial collagenase, which is functionally related to endogenous proteases in the human body, was used as a nucleating agent to induce the mineralization of zeolitic imidazolate framework-8 (ZIF-8) as a crystalline shell. This zinc-based MOF material was selected due to its remarkable stability under physiological conditions and good biocompatibility. The straightforward, water-based synthesis yielded microporous collagenase-embedded ZIF-8 particles. Once immobilized inside the biomimetically mineralized MOF, the protease presented limited catalytic activity, being ineffective in the proteolysis of a collagen-like peptide. In conclusion, biomimetic mineralization of ZIF-8 using collagenase not only provided immobilization of the enzyme, but also enabled the control of its activity. This synthetic approach provides a potentially useful concept in the prevention of proteolytic activity involved in the degradation of collagen matrices in living organisms.
- Published
- 2019
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