Wenger Marco P E, Bozec Laurent, Horton Michael A, Mesquida Patrick
Bone and Mineral Centre, Department of Medicine, London Centre for Nanotechnology, University College London, London, United Kingdom.
Biophys J. 2007 Aug 15;93(4):1255-63. doi: 10.1529/biophysj.106.103192. Epub 2007 May 25.
The formation of collagen fibers from staggered subfibrils still lacks a universally accepted model. Determining the mechanical properties of single collagen fibrils (diameter 50-200 nm) provides new insights into collagen structure. In this work, the reduced modulus of collagen was measured by nanoindentation using atomic force microscopy. For individual type 1 collagen fibrils from rat tail, the modulus was found to be in the range from 5 GPa to 11.5 GPa (in air and at room temperature). The hypothesis that collagen anisotropy is due to the subfibrils being aligned along the fibril axis is supported by nonuniform surface imprints performed by high load nanoindentation.
由交错排列的亚纤维形成胶原纤维的过程仍缺乏一个被普遍接受的模型。确定单个胶原纤维(直径50 - 200纳米)的力学性能为胶原结构提供了新的见解。在这项工作中,使用原子力显微镜通过纳米压痕测量了胶原蛋白的折合模量。对于来自大鼠尾巴的单个I型胶原纤维,发现其模量在5吉帕至11.5吉帕范围内(在空气中且室温下)。高负载纳米压痕产生的不均匀表面印记支持了胶原各向异性是由于亚纤维沿纤维轴排列的这一假设。