Revealing the secondary structural changes of amyloid β peptide by probing the spectral fingerprint characters

Authors

  • Qian Wang,

    1. Bowling Green State University, Department of Chemistry, Center for Photochemical Sciences, Bowling Green, OH, USA
    2. Xiamen University, Department of Chemistry, College of Chemistry and Chemical Engineering, Xiamen, China
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  • Yuanmin Wang,

    1. Bowling Green State University, Department of Chemistry, Center for Photochemical Sciences, Bowling Green, OH, USA
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  • H. Peter Lu

    Corresponding author
    • Bowling Green State University, Department of Chemistry, Center for Photochemical Sciences, Bowling Green, OH, USA
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Correspondence to: H. Peter Lu, Bowling Green State University, Department of Chemistry, Center for Photochemical Sciences, Bowling Green, OH 43403, USA.

E-mail: hplu@bgsu.edu

Abstract

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.

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