摘要
β淀粉样蛋白 (Aβ)是阿尔茨海默症 (AD)患者脑中斑块的核心蛋白 ,它由多种衍生自淀粉样前体蛋白(APP)的不同长度的肽组成 ,其中Aβ40和Aβ42是主要的组分。我们通过电镜研究了这两种蛋白的纤维形成过程。在溶液中Aβ42倾向于形成斑块状沉积 ,而Aβ40则更易于形成典型的纤维。这种不同可能由Aβ42的相对更为紧密的二级构象所致。根据这些数据 ,我们推测静电作用对于早期Aβ42聚集是非常重要的 。
β-Amyloid peptide (Aβ), the core protein of plaques of Alzheimer's disease (AD), is a mixture of multilength peptides which are all derived from the amyloid precursor protein (APP). Aβ1 40 and Aβ1 42 are the normal physiological component and the pathological peptide due to its easier aggregation character respectively. By means of transmission electron microscopy (TEM), we examined the fibril formation process of these two proteins. In the solution Aβ42 tends to forming the plaque like deposition, while Aβ40 is more apt to form typical fibrils. This distinctness may be caused by the more compact secondary conformation of Aβ42. Our data suggests that electrostatic interaction might be important for the initial aggregation of Aβ42, which could give hints to the understanding of different role of Aβ40 and Aβ42 in the amyloid formation.
出处
《电子显微学报》
CAS
CSCD
北大核心
2003年第1期21-25,共5页
Journal of Chinese Electron Microscopy Society
