Biological mineralization of tissues in living organisms relies on proteins that preferentially nucleate minerals and control their growth. This process is often referred to as "templating," but this term has become generic, denoting various proposed mineral-organic interactions including both chemical and structural affinities. Here, we present an approach using self-assembled networks of elastin and fibronectin fibers, similar to the extracellular matrix. When induced onto negatively charged sulfonated polystyrene surfaces, these proteins form fiber networks of approximately 10-mum spacing, leaving open regions of disorganized protein between them. We introduce an atomic force microscopy-based technique to measure the elastic modulus of both structured and disorganized protein before and during calcium carbonate mineralization. Mineral-induced thickening and stiffening of the protein fibers during early stages of mineralization is clearly demonstrated, well before discrete mineral crystals are large enough to image by atomic force microscopy. Calcium carbonate stiffens the protein fibers selectively without affecting the regions between them, emphasizing interactions between the mineral and the organized protein fibers. Late-stage observations by optical microscopy and secondary ion mass spectroscopy reveal that Ca is concentrated along the protein fibers and that crystals form preferentially on the fiber crossings. We demonstrate that organized versus unstructured proteins can be assembled mere nanometers apart and probed in identical environments, where mineralization is proved to require the structural organization imposed by fibrillogenesis of the extracellular matrix.

译文

:生物体内组织的生物矿化依赖蛋白质优先使矿物质成核并控制其生长。该过程通常被称为“模板化”,但该术语已变得通用,表示各种提议的矿物-有机相互作用,包括化学亲和力和结构亲和力。在这里,我们提出一种使用弹性蛋白和纤连蛋白纤维自组装网络的方法,类似于细胞外基质。当被诱导到带负电荷的磺化聚苯乙烯表面上时,这些蛋白质形成大约10微米间距的纤维网络,在它们之间留下了杂乱的蛋白质的开放区域。我们引入基于原子力显微镜的技术来测量碳酸钙矿化之前和期间结构化和无组织蛋白的弹性模量。在矿化的早期阶段,很明显地证明了矿物质诱导的蛋白质纤维的增厚和变硬,早在离散的矿物晶体足够大以至于无法通过原子力显微镜成像时。碳酸钙选择性地使蛋白质纤维变硬而不影响它们之间的区域,强调了矿物质和有组织的蛋白质纤维之间的相互作用。通过光学显微镜和二次离子质谱的后期观察显示,Ca沿着蛋白质纤维集中,并且晶体优先在纤维交叉处形成。我们证明有组织的与非结构化的蛋白质可以仅相隔纳米而组装在一起,并在相同的环境中进行探测,在该环境中,矿化被证明需要细胞外基质的原纤维形成所强加的结构组织。

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