Department of Chemistry, University of California, Irvine, Irvine, California 92697-2025, United States.
Biochemistry. 2011 Nov 15;50(45):9809-16. doi: 10.1021/bi201317c. Epub 2011 Oct 20.
Understanding the aggregation mechanism of amyloid fibrils and characterizing their structures are important steps in the investigation of several neurodegenerative disorders associated with the misfolding of proteins. We report a simulation study of coherent two-dimensional chiral signals of three NMR structures of Aβ protein fibrils associated with Alzheimer's Disease, two models for Aβ(8-40) peptide wild-type (WT) and one for the Iowa (D23N) Aβ(15-40) mutant. Both far-ultraviolet (FUV) signals (λ = 190-250 nm), which originate from the backbone nπ* and ππ* transitions, and near-ultraviolet (NUV) signals (λ ≥ 250 nm) associated with aromatic side chains (Phe and Tyr) show distinct cross-peak patterns that can serve as novel signatures for the secondary structure.
了解淀粉样纤维的聚集机制并对其结构进行表征，是研究与蛋白质错误折叠相关的几种神经退行性疾病的重要步骤。我们报告了一项关于与阿尔茨海默病相关的三种 Aβ 蛋白纤维的 NMR 结构的相干二维手性信号的模拟研究，这两个模型是 Aβ(8-40)肽野生型（WT）和一个爱荷华州（D23N）Aβ(15-40)突变体。远紫外（FUV）信号（λ = 190-250nm），源于骨架 nπ* 和 ππ* 跃迁，以及与芳香侧链（Phe 和 Tyr）相关的近紫外（NUV）信号（λ≥250nm）都表现出明显的交叉峰模式，可作为二级结构的新特征。
