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Soluble silicon patterns and templates: calcium phosphate nanocrystal deposition in collagen type 1

机译:可溶性硅图案和模板:1型胶原蛋白中的磷酸钙纳米晶体沉积

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摘要

Patterned mineralisation is a feature of many hard-tissues. The impressive mechanical properties exhibited by such tissues can be, in part, attributed to the patterned deposition of mineral within the organic matrix. Although not thermodynamically favourable, the deposition of calcium phosphate based mineral within collagen fibres occurs in vivo in bone and dentine. As a consequence, numerous researchers have investigated how matrix proteins may be conditioned to enable patterned mineral deposition to recapitulate the structures found in nature. In this study, we have demonstrated that this patterned mineralisation of collagen type I may be induced simply by the pretreatment of the collagen with orthosilicic acid (OSA). The OSA treatment of the collagen resulted in a structural change to the collagen fibres, modifying fibril diameter and changing the kinetics of fibre formation. NMR demonstrated that the OSA preferentially located to the termini of the procollagen fibrils, thereby templating the formation of apatitic calcium phosphate crystals within the collagen fibrils (as shown using TEM, EDX and SAED). This work demonstrates how simple inorganic ions can have potent effects on structuring biological precipitates and suggests why trace quantities of silicon ions are essential to the formation of healthy hard tissues.
机译:图案化矿化是许多硬组织的特征。这种组织表现出的令人印象深刻的机械性能可以部分归因于矿物在有机基质中的图案化沉积。尽管在热力学上不是有利的,但是胶原纤维内磷酸钙基矿物质的沉积在体内发生在骨骼和牙本质中。结果,许多研究人员研究了如何调节基质蛋白以使图案化的矿物质沉积能够概括自然界中存在的结构。在这项研究中,我们已经证明,通过用原硅酸(OSA)预处理胶原蛋白可以简单地诱导这种I型胶原蛋白的矿化。 OSA处理胶原蛋白导致胶原纤维的结构变化,改变了原纤维直径并改变了纤维形成的动力学。 NMR显示OSA优先位于原胶原纤维的末端,从而使胶原纤维中的磷灰石磷酸钙晶体形成模板(如使用TEM,EDX和SAED所示)。这项工作证明了简单的无机离子如何对构造生物沉淀物具有有效的作用,并说明了为什么微量的硅离子对于健康的硬组织的形成至关重要。

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