title: Probing amyloid fibril growth by two-dimensional near-ultraviolet spectroscopy.
abstract: Keeping track of the aggregation kinetics of amyloid fibrils is essential for understanding their formation mechanism and eventually developing treatments for misfolded protein-related diseases. A simulation study of a series of Aβ(9-40) amyloid fibrils with different size shows that novel two-dimensional near-ultraviolet (2DNUV) spectra contain characteristic signatures of interactions between peptides. Chiral 2DNUV signals show a larger degree of exciton delocalization compared to their nonchiral counterparts. Intensities of specific peaks provide a direct measure of the number of peptides in a fibril. These signals could be used to monitor the fibril growth kinetics, one peptide at a time.
authors.affiliation: Chemistry Department, University of California, Irvine, Irvine, California 92697, USA. jiangj1@uci.edu
authors.forename: Jun
authors.initials: J
authors.lastname: Jiang
authors.forename: Shaul
authors.initials: S
authors.lastname: Mukamel
mesh_terms: D000682:Amyloid / Q000737:chemistry*; D016229:Amyloid beta-Peptides / Q000737:chemistry* / Q000378:metabolism; D007700:Kinetics; D056004:Molecular Dynamics Simulation; D011789:Quantum Theory; D013056:Spectrophotometry, Ultraviolet
chemical_list: D000682:Amyloid; D016229:Amyloid beta-Peptides