Surface-enhanced Raman scattering sensing platform for detecting amyloid-β peptide interaction with an aggregation inhibitor

Marcos A. Soares de Oliveira; Silvia Hilt; Che Wei Chang; Changwon Lee; John C Voss; James W. Chan

doi:10.1364/AO.399307

Surface-enhanced Raman scattering sensing platform for detecting amyloid-β peptide interaction with an aggregation inhibitor

Marcos A. Soares de Oliveira, Silvia Hilt, Che Wei Chang, Changwon Lee, John C Voss, James W. Chan

Research output: Contribution to journal › Article › peer-review

Abstract

Soluble, small amyloid-β oligomers (AβO) 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-β (Aβ) 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 Aβ peptides and spin-labeled fluorine (SLF), a peptide aggregation inhibitor. Changes in the peak positions and intensity ratios of two spectral peaks near 1600 cm⁻1 and 2900 cm⁻¹ can be used to monitor the molecular interactions between SLF and Aβ. This study demonstrates the potential of SERS spectroscopy for rapidly screening and identifying new anti-Aβ therapeutic agents.

Original language	English (US)
Pages (from-to)	7490-7495
Number of pages	6
Journal	Applied Optics
Volume	59
Issue number	25
DOIs	https://doi.org/10.1364/AO.399307
State	Published - Sep 1 2020

ASJC Scopus subject areas

Atomic and Molecular Physics, and Optics
Engineering (miscellaneous)
Electrical and Electronic Engineering

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abstract = "Soluble, small amyloid-β oligomers (AβO) are recognized as significant contributors to the pathology of Alzheimer{\textquoteright}s disease (AD). Although drugs for treating AD symptoms have been approved, no therapy targeting amyloid-β (Aβ) 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 Aβ peptides and spin-labeled fluorine (SLF), a peptide aggregation inhibitor. Changes in the peak positions and intensity ratios of two spectral peaks near 1600 cm−1 and 2900 cm−1 can be used to monitor the molecular interactions between SLF and Aβ. This study demonstrates the potential of SERS spectroscopy for rapidly screening and identifying new anti-Aβ therapeutic agents.",

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AU - Soares de Oliveira, Marcos A.

AU - Hilt, Silvia

AU - Chang, Che Wei

AU - Lee, Changwon

AU - Voss, John C

AU - Chan, James W.

PY - 2020/9/1

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AB - Soluble, small amyloid-β oligomers (AβO) 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-β (Aβ) 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 Aβ peptides and spin-labeled fluorine (SLF), a peptide aggregation inhibitor. Changes in the peak positions and intensity ratios of two spectral peaks near 1600 cm−1 and 2900 cm−1 can be used to monitor the molecular interactions between SLF and Aβ. This study demonstrates the potential of SERS spectroscopy for rapidly screening and identifying new anti-Aβ therapeutic agents.

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Surface-enhanced Raman scattering sensing platform for detecting amyloid-β peptide interaction with an aggregation inhibitor

Abstract

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