Department of Chemistry and Biochemistry, University of California, San Diego, 9500 Gilman Drive, La Jolla, CA 92093-0358, USA.
ChemMedChem. 2010 Jan;5(1):56-60. doi: 10.1002/cmdc.200900440.
Alzheimer’s disease (AD) is characterized by a progressive loss of cognitive function and constitutes the most common and fatal neurodegenerative disorder.[1] Genetic and clinical evidence supports the hypothesis that accumulation of amyloid deposits in the brain plays an important role in the pathology of the disease. This event is associated with perturbations of biological functions in the surrounding tissue leading to neuronal cell death, thus contributing to the disease process. The deposits are comprised primarily of amyloid (Aβ) peptides, a 39–43 amino acid sequence that self aggregates into a fibrillar β-pleated sheet motif. While the exact three-dimensional structure of the aggregated Aβ peptides is not known, a model structure that sustains the property of aggregation has been proposed.[2] This creates opportunities for in vivo imaging of amyloid deposits that can not only help evaluate the time course and evolution of the disease, but can also allow the timely monitoring of therapeutic treatments.[3]
阿尔茨海默病（AD）的特征是认知功能进行性丧失，是最常见和最致命的神经退行性疾病。[1]遗传和临床证据支持这样一种假设，即大脑中淀粉样沉积的积累在疾病的病理中起着重要作用。这一事件与周围组织中生物功能的改变有关，导致神经元细胞死亡，从而促进了疾病的发展。沉积物主要由淀粉样（Aβ）肽组成，Aβ 肽是一个 39-43 个氨基酸序列，自身聚集形成纤维状 β-折叠片结构。虽然聚集的 Aβ 肽的确切三维结构尚不清楚，但已经提出了一种维持聚集特性的模型结构。[2]这为体内淀粉样沉积的成像创造了机会，不仅有助于评估疾病的时间过程和演变，还可以允许对治疗进行及时监测。[3]
