The University of Michigan Department of Chemistry, 930 North University Avenue, Ann Arbor, Michigan 48109-1055, USA.
Langmuir. 2010 May 18;26(10):7349-54. doi: 10.1021/la100006a.
This study demonstrates that collagen, the most abundant protein in animals, exists as a distribution of nanoscale morphologies in teeth, bones, and tendons. This fundamental characteristic of Type I collagen has not previously been reported and provides a new understanding of the nanoscale architecture of this ubiquitous and important biological nanomaterial. Dentin, bone, and tendon tissue samples were chosen for their differences in cellular origin and function, as well as to compare mineralized tissues with a tissue that lacks mineral in a normal physiological setting. A distribution of morphologies was present in all three tissues, confirming that this characteristic is fundamental to Type I collagen regardless of the presence of mineral, cellular origin of the collagen (osteoblast versus odontoblast versus fibroblast), anatomical location, or mechanical function of the tissue.
本研究表明,胶原蛋白作为动物体中含量最丰富的蛋白质,以纳米级形态分布存在于牙齿、骨骼和肌腱中。I 型胶原蛋白的这种基本特征以前尚未有报道,为理解这种普遍存在且重要的生物纳米材料的纳米级结构提供了新的认识。牙本质、骨骼和肌腱组织样本因细胞起源和功能的不同而被选择,以便在正常生理环境下比较矿化组织与缺乏矿物质的组织。所有三种组织中均存在形态分布,这证实了这种特征是 I 型胶原蛋白的基础,而与矿物质的存在、胶原蛋白的细胞起源(成骨细胞、成牙本质细胞还是成纤维细胞)、组织的解剖位置或机械功能无关。