High-resolution AFM imaging of intact and fractured trabecular bone
High-resolution AFM imaging of intact and fractured trabecular bone
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DOI：
10.1016/j.bone.2004.02.024
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发表时间：
2004-07-01
期刊：
影响因子：
4.1
通讯作者：
Hansma, PK
中科院分区：
文献类型：
--
作者：
Hassenkam, T;Fantner, GE;Hansma, PK
生物矿化材料的纳米级结构分析经常有助于阐明这些复杂的有机-无机复合材料中重要的结构-功能关系。原子力显微镜（AFM）对骨小梁外表面的成像显示胶原原纤维的紧密编织结构，以67 nm的周期性带状排列，以及密集排列的矿物板。胶原原纤维上的矿物板重叠，板直径范围从30到200圈不等。在胶原原纤维上，小结节状特征，间隔20- 30nm，垂直于原纤维。在某些情况下，这些结节也可见于胶原原纤维之间延伸的纤维。我们假设这些突起是非胶原蛋白，如蛋白聚糖，可能在样品干燥时坍塌成致密的结构。原始断裂表面的原子力显微镜图像显示了密集的矿物板阵列。在一些孤立的位置，可见裸露的胶原原纤维的短切面。在其他地区，胶原原纤维的存在可以从矿物板的线性模式推断出来。断裂的样品，冲洗以去除矿物板，在断裂的表面上显示分离的胶原纤维。这些原纤维通常覆盖着与外表面相似的突起，但组织较少。此外，与外表面一样，有时在相邻的胶原原纤维之间延伸出小纤维。这些研究为这种复杂生物复合材料的纳米结构提供了重要的见解。(C) 2004爱思唯尔公司版权所有。
Nanoscale structural analyses of biomineralized materials can frequently help elucidate important structure-function relationships in these complex organic-inorganic composites. Atomic force microscope (AFM) imaging of the exterior surface of trabecular bone reveals a densely woven structure of collagen fibrils, banded with a 67-nm periodicity, and densely packed mineral plates. The mineral plates on the collagen fibrils overlap and exhibit a large range of plate diameters from 30 to 200 rim. On the collagen fibrils, small nodular features, spaced 20-30 nm, run perpendicular to the fibrils. In some cases, these nodules are also seen on filaments extending between collagen fibrils. We hypothesize that these protrusions are noncollagenous proteins such as proteoglycans and may have collapsed into compact structures when the sample was dried. AFM images of pristine fractured surfaces reveal a dense array of mineral plates. In a few isolated locations, short sections of bare collagen fibrils are visible. In other regions, the existence of the underlying collagen fibrils can be inferred from the linear patterns of the mineral plates. Fractured samples, rinsed to remove mineral plates, reveal separated collagen fibrils on the fractured surfaces. These fibrils are often covered with protrusions similar to those observed on the exterior surfaces but are less organized. In addition, as on the exterior surfaces, there are sometimes small filaments extending between neighboring collagen fibrils. These studies provide important insights into the nanostructured architecture of this complex biocomposite. (C) 2004 Elsevier Inc. All rights reserved.