通过扫描隧道显微镜测定的人及大鼠胰岛淀粉样多肽β-折叠样结构特征。
Structural characteristics of the beta-sheet-like human and rat islet amyloid polypeptides as determined by scanning tunneling microscopy.
作者信息
Mao Xiaobo, Ma Xiaojing, Liu Lei, Niu Lin, Yang Yanlian, Wang Chen
机构信息
National Center for Nanoscience and Technology, Beijing 100190, China.
出版信息
J Struct Biol. 2009 Sep;167(3):209-15. doi: 10.1016/j.jsb.2009.05.009. Epub 2009 Jun 6.
We demonstrate in this work that scanning tunneling microscopy (STM) provides a useful approach to obtaining structural information about human islet amyloid polypeptide (hIAPP) and rat islet amyloid polypeptide (rIAPP) assembly on highly oriented pyrolytic graphite (HOPG) with sub-molecular resolution. The observed hIAPP and rIAPP lamellae consisted of parallel stripes. The STM images of hIAPPs show multiple molecular folding structures, with an average of 11 amino acid residues for the core regions. In addition, the STM images also reveal the assembly characteristics of rIAPP lamellae and may indicate a secondary structural conformation from random coil to beta-sheet-like on the graphite surface.
我们在这项工作中证明，扫描隧道显微镜（STM）提供了一种有用的方法，可在具有亚分子分辨率的高度定向热解石墨（HOPG）上获取有关人胰岛淀粉样多肽（hIAPP）和大鼠胰岛淀粉样多肽（rIAPP）组装的结构信息。观察到的hIAPP和rIAPP薄片由平行条纹组成。hIAPP的STM图像显示出多种分子折叠结构，核心区域平均有11个氨基酸残基。此外，STM图像还揭示了rIAPP薄片的组装特征，并可能表明在石墨表面上从无规卷曲到β-折叠样的二级结构构象。
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