The supramolecular structure of bone: X‐ray scattering analysis and lateral structure modeling

Zhou Hong-Wen; Burger Christian; Wang HaoHsiao Benjamin S.Chu BenjaminGraham Lila

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The supramolecular structure of bone: X‐ray scattering analysis and lateral structure modeling

机译：骨的超分子结构:X射线散射分析和横向结构建模

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The evolution of vertebrates required a key development in supramolecular evolution: internally mineralized collagen fibrils. In bone, collagen molecules and mineral crystals form a nanocomposite material comparable to cast iron in tensile strength, but several times lighter and more flexible. Current understanding of the internal nanoscale structure of collagen fibrils, derived from studies of rat tail tendon (RTT), does not explain how nucleation and growth of mineral crystals can occur inside a collagen fibril. Experimental obstacles encountered in studying bone have prevented a solution to this problem for several decades. This report presents a lateral packing model for collagen molecules in bone fibrils, based on the unprecedented observation of multiple resolved equatorial reflections for bone tissue using synchrotron small‐angle X‐ray scattering (SAXS; ～1?nm resolution). The deduced structure for pre‐mineralized bone fibrils includes features that are not present in RTT: spatially discrete microfibrils. The data are consistent with bone microfibrils similar to pentagonal Smith microfibrils, but are not consistent with the (nondiscrete) quasi‐hexagonal microfibrils reported for RTT. These results indicate that collagen fibrils in bone and tendon differ in their internal structure in a manner that allows bone fibrils, but not tendon fibrils, to internally mineralize. In addition, the unique pattern of collagen cross‐link types and quantities in mineralized tissues can be can be accounted for, in structural/functional terms, based on a discrete microfibril model.

机译：脊椎动物的进化所需的一个关键发展超分子进化:内部矿化胶原原纤维。胶原蛋白分子和矿物晶体组成纳米复合材料与铸铁轻、抗拉强度,但几次更加灵活。内部胶原原纤维的纳米结构,来自鼠尾肌腱(RTT)的研究,不能解释的成核和增长如何矿物晶体可以发生在一个胶原蛋白原纤维。研究骨阻止了一个解决方案几十年的问题。胶原蛋白分子的横向包装模式骨骼纤维,根据前所未有的观察多个解决赤道使用同步加速器反射的骨组织地理地理小角X射线散射(粉煤灰;分辨率)。提前矿化骨原纤维包括特性不存在于RTT:空间离散微纤维。微纤维类似于五角史密斯微纤维,但并不符合(nondiscrete)准‐microfibrils六角对RTT报道。在骨骼和肌腱胶原原纤维在不同其内部结构的方式,允许骨骼纤维,但不是腱纤维内部采集矿物。的胶原蛋白交叉链接类型和模式数量可以可以在矿化组织结构/功能而言,占基于离散微纤维模型。

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《Acta crystallographica. Section D, Structural biology.》 |2016年第9期|986-996|共11页
作者
Zhou Hong-Wen; Burger Christian; Wang HaoHsiao Benjamin S.Chu BenjaminGraham Lila;
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作者单位

Department of Chemistry, Stony Brook University, Stony Brook, NY11794-3400, USA;

Laboratory for the Study of Skeletal Disorders and Rehabilitation, Children's Hospital Boston;

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正文语种英语
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关键词
bone structure; Supramolecular structure; MicrofibrilsCollagenCollagen FibrilTendonFibrilround-trip delayStructural Modelslateral structure;

机译：骨骼结构;超分子结构;MicrofibrilsCollagenCollagenFibrilTendonFibrilround-trip delayStructuralModelslateral结构;

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The supramolecular structure of bone: X‐ray scattering analysis and lateral structure modeling

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