Bio-inspired Synthesis of Mineralized Collagen Fibrils.

Bio-inspired Synthesis of Mineralized Collagen Fibrils.
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DOI:
10.1021/cg800252f
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发表时间:
2008-08
影响因子:
3.8
通讯作者:
Beniash, Elia
Beniash, Elia
中科院分区:
化学2区
文献类型:
--
作者:
Deshpande, Atul S.;Beniash, Elia

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矿化胶原原纤维构成了牙本质、骨等胶原矿化组织的基本结构单位。了解胶原矿化机制对硬组织修复新材料的开发至关重要。我们使用聚l-天冬氨酸作为非胶原酸性蛋白质的类似物,对重建的胶原原纤维进行了仿生矿化。对反应产物的透射电镜和电子衍射研究显示,在原纤维中沉积了成堆的带状磷灰石晶体,其c轴与原纤维轴共排列。这种结构组织与骨和牙本质的矿化胶原蛋白非常相似。原纤维中形成的初始矿床缺乏长范围的结晶顺序,并随着时间的推移转变成晶体。有趣的是,这些无定形沉积物的形状和组织与成熟矿化原纤维中发现的晶体相似。我们证明胶原和聚l-天冬氨酸之间的相互作用对于矿化胶原原纤维的形成是必不可少的,而胶原单独不影响矿物的形成,聚l-天冬氨酸以浓度依赖的方式抑制矿化。这些结果为胶原矿化的基本机制提供了新的见解,并可能导致新型仿生纳米结构材料的发展。
Mineralized collagen fibrils constitute a basic structural unit of collagenous mineralized tissues such as dentin and bone. Understanding of the mechanisms of collagen mineralization is vital for development of new materials for the hard tissue repair. We carried out bio-inspired mineralization of reconstituted collagen fibrils using poly-l-aspartic acid, as an analog of non-collagenous acidic proteins. Transmission electron microscopy and electron diffraction studies of the reaction products revealed stacks of ribbon-shaped apatitic crystals, deposited within the fibrils with their c-axes co-aligned with the fibril axes. Such structural organization closely resembles mineralized collagen of bone and dentin. Initial mineral deposits formed in the fibrils lacked a long range crystallographic order and transformed into crystals with time. Interestingly, the shape and organization of these amorphous deposits was similar to the crystals found in the mature mineralized fibrils. We demonstrate that the interactions between collagen and poly-l-aspartic acid are essential for the mineralized collagen fibrils formation, while collagen alone does not affect mineral formation and poly-l-aspartic acid inhibits mineralization in a concentration dependant manner. These results provide new insights into basic mechanisms of collagen mineralization and can lead to the development of novel bio-inspired nanostructured materials.
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