title: Distinguishing amyloid fibril structures in Alzheimer's disease (AD) by two-dimensional ultraviolet (2DUV) spectroscopy.
abstract: 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.
authors.affiliation: Department of Chemistry, University of California, Irvine, Irvine, California 92697-2025, United States. alamng@uci.edu
authors.forename: A R
authors.initials: AR
authors.lastname: Lam
authors.forename: J
authors.initials: J
authors.lastname: Jiang
authors.forename: S
authors.initials: S
authors.lastname: Mukamel
mesh_terms: D000544:Alzheimer Disease / Q000235:genetics / Q000378:metabolism*; D000595:Amino Acid Sequence; D016229:Amyloid beta-Peptides / Q000737:chemistry* / Q000235:genetics; D002942:Circular Dichroism; D006801:Humans; D008958:Models, Molecular; D056004:Molecular Dynamics Simulation; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D017510:Protein Folding; D017433:Protein Structure, Secondary; D013056:Spectrophotometry, Ultraviolet
chemical_list: D016229:Amyloid beta-Peptides