In Situ Monitoring the Aggregation Dynamics of Amyloid-β Protein Aβ42 in Physiological Media via a Raman-Based Frequency Shift Method

Zhu, Wenfeng; Wang, Yibing; Xie, Dan; Cheng, Linxiu; Wang, Ping; Zeng, Qingdao; Li, Min; Zhao, Yuliang

doi:10.1021/acsabm.8b00257

Cited by 23 publications

(24 citation statements)

References 59 publications

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“…Applications of SERS frequency-shift sensing beyond isolated molecular/ionic sensing have also been uncovered. For example, the SERS spectral shifts of a Raman reporter (DSNB) upon amyloid-β (Aβ) protein binding were recorded for both in situ Aβ42 aggregation monitoring and for Aβ42 monomer and fiber detection . To do this, two affinity peptides were selected by biopanning and used for the specific binding of Aβ42 monomers and fibers, respectively (Figure a).…”

Section: Applications Of Sers Frequency-shift Assaysmentioning

confidence: 99%

Frequency Shift Surface-Enhanced Raman Spectroscopy Sensing: An Ultrasensitive Multiplex Assay for Biomarkers in Human Health

et al. 2021

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The sensitive and selective detection of biomarkers for human health remains one of the grand challenges of the analytical sciences. Compared to established methods (colorimetric, (chemi) luminescent), surface-enhanced Raman spectroscopy (SERS) is an emerging alternative with enormous potential for ultrasensitive biological detection. Indeed even attomolar (10 −18 M) detection limits are possible for SERS due to an orders-ofmagnitude boosting of Raman signals at the surface of metallic nanostructures by surface plasmons. However, challenges remain for SERS assays of large biomolecules, as the largest enhancements require the biomarker to enter a "hot spot" nanogap between metal nanostructures. The frequency-shift SERS method has gained popularity in recent years as an alternative assay that overcomes this drawback. It measures frequency shifts in intense SERS peaks of a Raman reporter during binding events on biomolecules (protein coupling, DNA hybridization, etc.) driven by mechanical transduction, charge transfer, or local electric field effects. As such, it retains the excellent multiplexing capability of SERS, with multiple analytes being identifiable by a spectral fingerprint in a single read-out. Meanwhile, like refractive index surface plasmon resonance methods, frequency-shift SERS measures the shift of an intense signal rather than resolving a peak above noise, easing spectroscopic resolution requirements. SERS frequency-shift assays have proved particularly suitable for sensing large, highly charged biomolecules that alter hydrogen-bonding networks upon specific binding. Herein we discuss the frequency-shift SERS method and promising applications in (multiplex) biomarker sensing as well as extensions to ion and gas sensing and much more.

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Section: Applications Of Sers Frequency-shift Assaysmentioning

confidence: 99%

Frequency Shift Surface-Enhanced Raman Spectroscopy Sensing: An Ultrasensitive Multiplex Assay for Biomarkers in Human Health

et al. 2021

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“…As the deformation-induced frequency shift is independent of the magnitude of SERS intensity, it can be used as an independent and potentially more robust optical transducer in complementary to the prevailing intensity-based signal readout. Despite its promise, the SERS frequency shiftbased strategy has been surprisingly underappreciated, with only a handful of proof-of-concept studies that were built on this method for detection of proteins, [30][31][32] circulating tumor DNA, [33] and serum microRNA. [34][35] Notably, the studied analytes using the SERS frequency shift method belong to the category of macromolecules rather than small molecules, presumably because of the limited structural deformation experienced by antibody-conjugated Raman reporters after capturing small molecules.…”

Section: Introductionmentioning

confidence: 99%

A Dual‐Modal Single‐Antibody Plasmonic Spectro‐Immunoassay for Detection of Small Molecules

Zheng

Raj

et al. 2022

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Small molecules play a pivotal role in regulating physiological processes and serve as biomarkers to uncover pathological conditions and the effects of therapeutic treatments. However, it remains a significant challenge to detect small molecules given the size as compared to macromolecules. Recently, the newly emerging plasmonic immunoassays based on surface‐enhanced Raman scattering (SERS) offer great promise to deliver extraordinary sensitivity. Nevertheless, they are limited by the intrinsic SERS intensity fluctuations associated with the SERS uncertainty principle. The single transducer that relies on the intensity change is also prone to false signals. Additionally, the prevailing sandwich immunoassay format proves less effective towards detecting small molecules. To circumvent these critical issues, a dual‐modal single‐antibody approach that synergizes both the intensity and shift of the peak‐based immunoassay with Raman enhancement, coined as the INSPIRE assay, is developed for small molecules detection. With two independent transduction mechanisms, it allows better prediction of analyte concentration and attenuation of signal artifacts, providing a new and robust strategy for molecular analysis. With a proof‐of‐concept demonstration for detection of free T4 and testosterone in serum matrix, the authors envision that the INSPIRE assay could be expanded for a wide spectrum of applications in biomedical diagnosis, discovery of new biopharmaceuticals, food safety, and environmental monitoring.

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“…Many attempts have been made to explore new diagnostic tools for several core biomarkers, including enzyme-linked immunosorbent assay (ELISA) [34][35][36], nanoparticle-based immunoassays [37], electrochemistry [38], surface-enhanced Raman spectroscopy [39,40], fluorescence [41], and electrochemical biosensors [42,43]. However, due to the heterogeneity and transient nature of Aβ oligomers, most of these assays not only cannot distinguish between Aβ 42 Os and Aβ 42 Ms but also require equipment or/and expertise.…”

Section: Introductionmentioning

confidence: 99%

Quantitative assessment of AD markers using naked eyes: point-of-care testing with paper-based lateral flow immunoassay

Zhang

et al. 2021

J Nanobiotechnol

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Aβ42 is one of the most extensively studied blood and Cerebrospinal fluid (CSF) biomarkers for the diagnosis of symptomatic and prodromal Alzheimer’s disease (AD). Because of the heterogeneity and transient nature of Aβ42 oligomers (Aβ42Os), the development of technologies for dynamically detecting changes in the blood or CSF levels of Aβ42 monomers (Aβ42Ms) and Aβ42Os is essential for the accurate diagnosis of AD. The currently commonly used Aβ42 ELISA test kits usually mis-detected the elevated Aβ42Os, leading to incomplete analysis and underestimation of soluble Aβ42, resulting in a comprised performance in AD diagnosis. Herein, we developed a dual-target lateral flow immunoassay (dLFI) using anti-Aβ42 monoclonal antibodies 1F12 and 2C6 for the rapid and point-of-care detection of Aβ42Ms and Aβ42Os in blood samples within 30 min for AD diagnosis. By naked eye observation, the visual detection limit of Aβ42Ms or/and Aβ42Os in dLFI was 154 pg/mL. The test results for dLFI were similar to those observed in the enzyme-linked immunosorbent assay (ELISA). Therefore, this paper-based dLFI provides a practical and rapid method for the on-site detection of two biomarkers in blood or CSF samples without the need for additional expertise or equipment. Graphical Abstract

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In Situ Monitoring the Aggregation Dynamics of Amyloid-β Protein Aβ42 in Physiological Media via a Raman-Based Frequency Shift Method

Cited by 23 publications

References 59 publications

Frequency Shift Surface-Enhanced Raman Spectroscopy Sensing: An Ultrasensitive Multiplex Assay for Biomarkers in Human Health

Frequency Shift Surface-Enhanced Raman Spectroscopy Sensing: An Ultrasensitive Multiplex Assay for Biomarkers in Human Health

A Dual‐Modal Single‐Antibody Plasmonic Spectro‐Immunoassay for Detection of Small Molecules

Quantitative assessment of AD markers using naked eyes: point-of-care testing with paper-based lateral flow immunoassay

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