Surface-enhanced Raman spectroscopy for detection of toxic amyloid β oligomers adsorbed on self-assembled monolayers

Voiciuk, Vladislava; Valinčius, Gintaras; Budvytytė, Rima; Matijoška, Algirdas; Matulaitienė, Ieva; Niaura, Gediminas

doi:10.1016/j.saa.2012.04.043

Cited by 25 publications

(23 citation statements)

References 47 publications

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“…6,7 Western blot is a semiquantitative method for special recognition of AβO. 8,9 Examples of quantitative analysis are enzyme-linked immunosorbent assay (ELISA), 10 fluorescent assays, 11,12 surface-enhanced Raman spectroscopy, 13 flow cytometry, 14 surface plasmon resonance nanosensor, 15 and so on. The abovementioned methods usually need expensive monoclonal antibodies, fluorescent dye, or sophisticated instruments.…”

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confidence: 99%

A hydrogel biosensor for high selective and sensitive detection of amyloid-beta oligomers

Sun

Zhong

Gui

et al. 2018

IJN

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Background Alzheimer’s disease (AD) is a neurodegenerative disorder characterized by progressive cognitive and memory impairment. It is the most common neurological disease that causes dementia. Soluble amyloid-beta oligomers (AβO) in blood or cerebrospinal fluid (CSF) are the pathogenic biomarker correlated with AD. Methods A simple electrochemical biosensor using graphene oxide/gold nanoparticles (GNPs) hydrogel electrode was developed in this study. Thiolated cellular prion protein (PrP C ) peptide probe was immobilized on GNPs of the hydrogel electrode to construct an AβO biosensor. Electrochemical impedance spectroscopy was utilized for AβO analysis. Results The specific binding between AβO and PrP C probes on the hydrogel electrode resulted in an increase in the electron-transfer resistance. The biosensor showed high specificity and sensitivity for AβO detection. It could selectively differentiate AβO from amyloid-beta (Aβ) monomers or fibrils. Meanwhile, it was highly sensitive to detect as low as 0.1 pM AβO in artificial CSF or blood plasma. The linear range for AβO detection is from 0.1 pM to 10 nM. Conclusion This biosensor could be used as a cost-effective tool for early diagnosis of AD due to its high electrochemical performance and bionic structure.

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confidence: 99%

A hydrogel biosensor for high selective and sensitive detection of amyloid-beta oligomers

Sun

Zhong

Gui

et al. 2018

IJN

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Section: Resultsmentioning

confidence: 99%

“…We finally performed a SERS characterization on amyloid aggregates, which show a marked heterogeneity and metastability complicating their structural analysis by standard structural biology techniques, [57] as well as by spectroscopic methods, including plasmon-enhanced spectroscopies. [58][59][60][61][62] Figure 7d shows the on-spot SERS spectrum obtained by drop deposition on a AgNWs@PTFE substrate of β-amyloid peptide Aβ 42 oligomers (see Table S5, Supporting Information for peak assignments), which are associated with Alzheimer's disease (AD) and a well recognised biomarker of the cerebrospinal fluid of AD patients. Here, strong peaks emerge in the SERS spectrum: 940 cm À 1 (ν CH2 ), 1003 and 1030 cm À 1 (Phe), 1049 cm À 1 (ν CN ), 1454 cm À 1 (δ CH2,CH3 ) and 1605 cm À 1 (Tyr, Phe) while less intense spectral features are observed at 1115 and 1126 cm À 1 (ν CCN , δ NH3 + ), 1430 cm À 1 (Tyr), 1498 cm À 1 (His) and 1582 cm À 1 (Tyr, Phe).…”

Section: Resultsmentioning

confidence: 99%

Spot‐on SERS Detection of Biomolecules with Laser‐Patterned Dot Arrays of Assembled Silver Nanowires

et al. 2019

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Unique characteristics of SERS including the possibility to reveal the compositional and structural content of trace amounts of biological samples without any pre‐treatment, depict this technique as a promising label‐free alternative to standard analytical methods. Despite significant advancements, current SERS substrates for biomolecule detection suffer from a number of issues still impeding their routine usage and commercial exploitation, including complex and expensive fabrication procedures and scarce standardization perspectives. Herein a combined bottom up/top down scheme based on flow‐through method plus laser patterning is proposed to prepare dot arrays of silver nanowires on a hydrophobic substrate for catching the analyte content from a minute amount of liquid sample and its rapid SERS inspection. As a consequence, a simple spot‐on analysis specifically adapted for reliable identification and characterization of molecules of biomedical interest is made possible. Our attempt may represent a concrete chance for progressing SERS toward widespread commercially viable sensing applications including diagnostics at the point‐of‐need settings and on‐site analyses.

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“…Voiciuk et al . adsorbed oligomeric forms of Aβ42 onto self‐assembled monolayers terminated by heptanethiol, octadecanethiol, or N‐(6‐mercapto)pyridinium groups in an effort to detect unique spectral features . Changes in carboxylate stretching modes were observed upon binding.…”

Section: Introductionmentioning

confidence: 99%

“…6,8 Voiciuk et al adsorbed oligomeric forms of Ab42 onto self-assembled monolayers terminated by heptanethiol, octadecanethiol, or N-(6-mercapto)pyridinium groups in an effort to detect unique spectral features. 9 Changes in carboxylate stretching modes were observed upon binding. Most recently, Nabers et al suggested that spectral shifts in the amide I band of Ab in cerebrospinal fluid might discriminate dementia of the Alzheimer's disease type from other types of dementia.…”

Section: Introductionmentioning

confidence: 99%

Surface enhanced Raman spectroscopy distinguishes amyloid Β‐protein isoforms and conformational states

Hayden

Xia

et al. 2018

Protein Science

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Amyloid β-protein (Aβ) self-association is one process linked to the development of Alzheimer's disease (AD). Aβ peptides, including its most abundant forms, Aβ40 and Aβ42, are associated with the two predominant neuropathologic findings in AD, vascular and parenchymal amyloidosis, respectively. Efforts to develop therapies for AD often have focused on understanding and controlling the assembly of these two peptides. An obligate step in these efforts is the monitoring of assembly state. We show here that surface-enhanced Raman spectroscopy (SERS) coupled with principal component analysis (PCA) readily distinguishes Aβ40 and Aβ42. We show further, through comparison of assembly dependent changes in secondary structure and morphology, that the SERS/PCA approach unambiguously differentiates closely related assembly stages not readily differentiable by circular dichroism spectroscopy, electron microscopy, or other techniques. The high discriminating power of SERS/PCA is based on the rich structural information present in its spectra, which comprises not only on interatomic resonances between covalently associated atoms and hydrogen bond interactions important in controlling secondary structure, but effects of protein orientation relative to the substrate surface. Coupled with the label-free, single molecule sensitivity of SERS, the approach should prove useful for determining structure activity relationships, suggesting target sites for drug development, and for testing the effects of such drugs on the assembly process. The approach also could be of value in other systems in which assembly dependent changes in protein structure correlate with the formation of toxic peptide assemblies.

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Surface-enhanced Raman spectroscopy for detection of toxic amyloid β oligomers adsorbed on self-assembled monolayers

Cited by 25 publications

References 47 publications

A hydrogel biosensor for high selective and sensitive detection of amyloid-beta oligomers

A hydrogel biosensor for high selective and sensitive detection of amyloid-beta oligomers

Spot‐on SERS Detection of Biomolecules with Laser‐Patterned Dot Arrays of Assembled Silver Nanowires

Surface enhanced Raman spectroscopy distinguishes amyloid Β‐protein isoforms and conformational states

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