Aragno I, Odetti P, Altamura F, Cavalleri O, Rolandi R
Department of Internal Medicine (DiMI), University of Genova, Italy.
Experientia. 1995 Nov 15;51(11):1063-7. doi: 10.1007/BF01946917.
The Atomic Force Microscope (AFM) was used to inspect collagen fibrils deposited on mica sheets at different fibrillogenesis times. Collagen was obtained from rat tail tendon fibers. Various fibril forms were observed, together with the characteristic periodic intra-fibril structure (D-bands). The fibril thickness, width, D-band periodicity and depth were measured and the statistical distribution of these parameters at 1, 2, 5, 10 and 15 days of in vitro fibril formation time was calculated. The fibrils showed an increasing size with time, but the band interval measure remained stable. The band depth, after an initial increase, exhibited a relative steadiness. The results indicate that AFM offers, at low resolution, images qualitatively similar to those obtained with electron microscopy, but with less manipulation of the sample. A quantitative evaluation of collagen structural features in the nanometer scale is made possible by AFM.
原子力显微镜（AFM）用于检查在不同原纤维形成时间沉积在云母片上的胶原纤维。胶原蛋白取自大鼠尾腱纤维。观察到了各种纤维形态以及特征性的纤维内周期性结构（D带）。测量了纤维的厚度、宽度、D带周期和深度，并计算了在体外原纤维形成时间1、2、5、10和15天时这些参数的统计分布。纤维尺寸随时间增加，但带间隔测量保持稳定。带深度在最初增加后表现出相对稳定。结果表明，AFM在低分辨率下提供的图像在质量上与电子显微镜获得的图像相似，但对样品的操作较少。AFM使得对纳米尺度胶原蛋白结构特征进行定量评估成为可能。
