Investigations into the polymorphism of rat tail tendon fibrils using atomic force microscopy.
Investigations into the polymorphism of rat tail tendon fibrils using atomic force microscopy.
复制标题
使用原子力显微镜研究大鼠尾腱原纤维的多态性。
DOI：
10.1016/s0006-291x(03)00390-5
复制
发表时间：
2003
影响因子：
3.1
通讯作者：
Hansma,PaulK
中科院分区：
文献类型：
--
作者：
Venturoni,Manuela;Gutsmann,Thomas;Fantner,GeorgE;Kindt,JohannesH;Hansma,PaulK
当通过原子力或透射电子显微镜成像观察时，I 型胶原蛋白显示出 67 nm 的典型带状周期性。我们使用原子力显微镜在不同的离子和 pH 条件下研究了从大鼠尾腱中提取的胶原纤维。大多数纤维再现了典型的波状结构，间距为 67 nm，峰与槽之间的高度差至少为 5 nm。然而，我们还能够区分出另外两种周期性为 23±2nm 和 210±15nm 的带状图案。小图案显示出约2nm的高度差，而大图案似乎是67nm周期性的叠加，显示出约20nm的高度差。此外，我们还可以证明，在 pH 值 3 及以下时，原纤维结构会溶解，而高浓度的 NaCl 和 CaCl2 可以防止这种效应。
Collagen type I displays a typical banding periodicity of 67nm when visualized by atomic force or transmission electron microscopy imaging. We have investigated collagen fibers extracted from rat tail tendons using atomic force microscopy, under different ionic and pH conditions. The majority of the fibers reproduce the typical wavy structure with 67nm spacing and a height difference between the peak and the grooves of at least 5nm. However, we were also able to individuate two other banding patterns with 23±2nm and 210±15nm periodicities. The small pattern showed height differences of about 2nm, whereas the large pattern seems to be a superposition of the 67nm periodicity showing height differences of about 20nm. Furthermore, we could show that at pH values of 3 and below the fibril structure gets dissolved whereas high concentrations of NaCl and CaCl2could prevent this effect.