Fujita Y, Kobayashi K, Hoshino T
Equipment Centre for Research and Education, Nagoya University School of Medicine, Japan.
J Electron Microsc (Tokyo). 1997;46(4):321-6. doi: 10.1093/oxfordjournals.jmicro.a023526.
Three-dimensional structures of laterally aggregated bundles of collagen molecules, segment-long-spacing (SLS) crystallites, were imaged by atomic force microscopy (AFM) in atmosphere. The overall image of the type I collagen SLS in a height-amplified mode was semi-cylindrical, approximately 300 nm in length, with two bands of elevation near both N- and C- ends of the molecule. Its 'cross-sectional' profile (across the molecular axis) was a smooth arch. The 'axial' profile (along the molecular axis) had two prominent peaks approximately 250 nm apart, corresponding to the two bands of elevation. There were several minor peaks between these two prominent peaks. The elevation near both ends may be due to the presence of covalently bound sugars near both N- and C- ends of the helical part of type I collagen alpha chains. The AFM images of SLS presented here indicate that the type I collagen molecule is not uniform in diameter and has two bulged parts within its triple helix.
通过原子力显微镜(AFM)在大气环境下对横向聚集的胶原分子束——段长间距(SLS)微晶的三维结构进行了成像。在高度放大模式下,I型胶原SLS的整体图像呈半圆柱形,长度约为300nm,在分子的N端和C端附近有两条隆起带。其“横截面”轮廓(沿分子轴)是一个平滑的拱形。“轴向”轮廓(沿分子轴)有两个相距约250nm的突出峰,对应于两条隆起带。在这两个突出峰之间有几个较小的峰。两端附近的隆起可能是由于I型胶原α链螺旋部分的N端和C端附近存在共价结合的糖。此处呈现的SLS的AFM图像表明,I型胶原分子的直径并不均匀,并且在其三螺旋结构中有两个凸起部分。