DESCRIPTION: The amyloidogenesis of the amyloid-b (Ab) fibril is believed to be the cause of Alzheimer’s disease. We propose to use novel coherent nonlinear optical spectroscopy to study the fibril structure, which is crucial for the investigation of the toxicity and the aggregation procedure and is not fully characterized yet. We report a simulation study of the two dimensional Infrared (2DIR) signals of two most known NMR-determined models of Ab based on a molecular dynamics simulation combined with the Nonlinear Exciton Equations (NEE) formalism. The signals of the native and of various isotopically labeled samples are compared for both models. Specific spectroscopic signatures of different aggregate structures are identified.
REFERENCE: W.Zhuang, D. Abramavicius, D.Voronine and S. Mukamel “Discrimination of Structural Models of Amyloid Fibrils Using Two Dimensional Infrared Spectroscopy” (submitted to SCIENCE)