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Abstract:
The dense hierarchical structure of the extracellular matrix (ECM) of native bone cells is difficult to precisely replicate in synthetic scaffolds. This study proposes a strategy based on macromolecular crowding (MMC) to mimic the complex organic-inorganic interface of native bone ECM. Using amyloid proteins formed by phase transition lysate (PTL) as the organic matrix, the study simulates the crowded microenvironment under physiological conditions through reverse dialysis, inducing protein aggregation, conformational rearrangement, and liquid crystalline phase transition. Simultaneously, it promotes the reconstruction of the organic-inorganic interface and energy reorganization, ultimately constructing an amyloid-mineral mixed scaffold with structural stability, mechanical robustness, and biological activity. This provides a new paradigm for the design of bone tissue engineering scaffolds.
01 Research Background
The extracellular matrix (ECM) of native bone consists of collagen fibers and hydroxyapatite (HAp) nanocrystals, forming a dense hierarchical structure. These components jointly provide mechanical strength and biological functions to the bone. However, the challenge of faithfully replicating this complex organic-inorganic interface in synthetic scaffolds has long hindered the development of bone tissue engineering materials.
02 Main Content
This study focuses on addressing the core challenge of constructing the organic-inorganic interface of synthetic scaffolds that mimics native bone ECM. It proposes a scaffold preparation strategy driven by macromolecular crowding (MMC). Using amyloid proteins formed by phase transition lysate (PTL) as the organic matrix, the study simulates the crowded microenvironment of native bone ECM through reverse dialysis. It regulates the aggregation behavior, conformational rearrangement, and phase transition of amyloid proteins, while promoting the reconstruction of the organic-inorganic interface and energy reorganization. Ultimately, it achieves efficient biomineralization and constructs an amyloid-mineral mixed scaffold.
03 Research Design
The macromolecular crowding (MMC) strategy was adopted. Phase transition lysate (PTL) was selected as the source of amyloid protein. The crowded microenvironment of native bone ECM was simulated through reverse dialysis. This microenvironment induced the aggregation, conformational rearrangement, and liquid crystalline phase transition of amyloid proteins, simultaneously driving the reconstruction of the organic-inorganic interface and energy reorganization. The final goal was to engineer the amyloid-mineral mixed scaffold and verify its performance through in vitro and in vivo experiments.
04 Results
The constructed amyloid-mineral mixed scaffold exhibits excellent structural stability and mechanical robustness, while also having good biological activity. Its support for bone regeneration can be comparable to mineralized collagen protein, confirming the effectiveness of the macromolecular crowding-driven strategy in the preparation of bone tissue engineering scaffolds and the feasibility of using amyloid proteins as an organic matrix alternative to collagen.
05 Extension of Ideas
This study breaks away from the traditional approach of rich water dilution for scaffold preparation and establishes the application value of the macromolecular crowding strategy in biomimetic material synthesis. It not only provides a more biomimetic design concept for bone tissue engineering scaffolds but also lays the foundation for the expanded application of amyloid proteins in the field of biomaterials. At the same time, it provides a new direction for studying the regulation of material structure and function by mimicking physiological microenvironments.
