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[摘要]：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 A beta protein fibrils associated with Alzheimer's Disease, two models for A beta(8-40) peptide wild-type (WT) and one for the Iowa (D23N) A beta(15-40) mutant. Both far-ultraviolet (FUV) signals (lambda = 190-250 nm), which originate from the backbone n pi* and pi pi* transitions, and near-ultraviolet (NUV) signals (lambda >= 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. |
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