Abstract

Soluble, small amyloid-$\beta$ oligomers (${\rm{A}}\beta {\rm{O}}$) are recognized as significant contributors to the pathology of Alzheimer’s disease (AD). Although drugs for treating AD symptoms have been approved, no therapy targeting amyloid-$\beta$ (${\rm{A}}\beta$) capable of modifying the course of the disease is available. In an effort to develop a label-free method for screening new anti-AD therapeutic agents, we show the use of a surface-enhanced Raman scattering (SERS) active substrate for detecting the interactions between ${\rm{A}}\beta$ peptides and spin-labeled fluorine (SLF), a peptide aggregation inhibitor. Changes in the peak positions and intensity ratios of two spectral peaks near ${{1600}}\;{\rm{c}}{{\rm{m}}^{- 1}}$ and ${{2900}}\;{\rm{c}}{{\rm{m}}^{- 1}}$ can be used to monitor the molecular interactions between SLF and ${\rm{A}}\beta$. This study demonstrates the potential of SERS spectroscopy for rapidly screening and identifying new anti-${\rm{A}}\beta$ therapeutic agents.

© 2020 Optical Society of America

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