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Revealing the secondary structural changes of amyloid β peptide by probing the spectral fingerprint characters
Author(s) -
Wang Qian,
Wang Yuanmin,
Lu H. Peter
Publication year - 2013
Publication title -
journal of raman spectroscopy
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.748
H-Index - 110
eISSN - 1097-4555
pISSN - 0377-0486
DOI - 10.1002/jrs.4253
Subject(s) - thioflavin , raman spectroscopy , chemistry , amyloid (mycology) , biophysics , fingerprint (computing) , atomic force microscopy , peptide , microscopy , amyloid β , protein aggregation , fluorescence , protein secondary structure , protein folding , nanotechnology , biochemistry , alzheimer's disease , materials science , biology , optics , pathology , physics , disease , medicine , inorganic chemistry , computer security , computer science
The misfolding and aggregation of amyloid β (1‐42) peptide is crucial for a mechanical understanding of the formation of Alzheimer's disease. To investigate the detailed aggregation pathway and mechanism, it is important to identify the secondary structures of different aggregation forms. Here, we report probing different amyloid β aggregations in real time by using correlated approaches such as shell‐isolated surface‐enhanced Raman spectroscopy, thioflavin T fluorescence assay, and atomic force microscopy imaging. Our experimental results of Raman shifts have been further demonstrated by theoretical calculation, which indicates that the Raman spectral fingerprint changes are originated from the amyloid β secondary structure changes. Copyright © 2013 John Wiley & Sons, Ltd.