Laboratoire Chimie de la Matière Condensée de Paris, UMR 7574 CNRS, Université Pierre et Marie Curie, Collège de France, 11 place Marcelin Berthelot, 75231 Paris Cedex 05, France.
Nat Mater. 2012 Jul 1;11(8):724-33. doi: 10.1038/nmat3362.
The involvement of collagen in bone biomineralization is commonly admitted, yet its role remains unclear. Here we show that type I collagen in vitro can initiate and orientate the growth of carbonated apatite mineral in the absence of any other vertebrate extracellular matrix molecules of calcifying tissues. We also show that the collagen matrix influences the structural characteristics on the atomic scale, and controls the size and the three-dimensional distribution of apatite at larger length scales. These results call into question recent consensus in the literature on the need for Ca-rich non-collagenous proteins for collagen mineralization to occur in vivo. Our model is based on a collagen/apatite self-assembly process that combines the ability to mimic the in vivo extracellular fluid with three major features inherent to living bone tissue, that is, high fibrillar density, monodispersed fibrils and long-range hierarchical organization.
胶原蛋白在骨生物矿化中的作用已得到广泛认可,但它的具体作用仍不清楚。在这里,我们证明了在没有任何其他脊椎动物钙化组织细胞外基质分子的情况下,I 型胶原蛋白可以在体外启动和定向碳酸磷灰石的生长。我们还表明,胶原蛋白基质会影响原子尺度上的结构特征,并控制磷灰石在较大长度尺度上的大小和三维分布。这些结果对文献中关于富含钙的非胶原蛋白对于体内胶原蛋白矿化发生的必要性的最新共识提出了质疑。我们的模型基于胶原蛋白/磷灰石的自组装过程,该过程结合了模拟体内细胞外液的能力以及活骨组织所固有的三个主要特征,即高纤维密度、单分散纤维和长程分级组织。