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

Yu, Xinke; Hayden, Eric Y.; Xia, Ming; Liang, Owen; Cheah, Lisa; Teplow, David B.; Xie, Ya‐Hong

doi:10.1002/pro.3434

Cited by 39 publications

(24 citation statements)

References 26 publications

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“…Thus, if several types of amyloid aggregates may exist simultaneously in the neuron, new approaches are required. Label‐free methods such as surface‐enhanced Raman spectroscopy have been used to study the structure of synthetic Aβ fibrils18 and amyloid plaques in brain tissue,19 however, when applied to a single cell, low signal to noise ratio, high autofluorescence, and irreversible photodamage20 make it challenging to reveal molecular structures at the subcellular level.…”

Section: Introductionmentioning

confidence: 99%

Super‐Resolution Infrared Imaging of Polymorphic Amyloid Aggregates Directly in Neurons

et al. 2020

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Loss of memory during Alzheimer's disease (AD), a fatal neurodegenerative disorder, is associated with neuronal loss and the aggregation of amyloid proteins into neurotoxic β‐sheet enriched structures. However, the mechanism of amyloid protein aggregation is still not well understood due to many challenges when studying the endogenous amyloid structures in neurons or in brain tissue. Available methods either require chemical processing of the sample or may affect the amyloid protein structure itself. Therefore, new approaches, which allow studying molecular structures directly in neurons, are urgently needed. A novel approach is tested, based on label‐free optical photothermal infrared super‐resolution microspectroscopy, to study AD‐related amyloid protein aggregation directly in the neuron at sub‐micrometer resolution. Using this approach, amyloid protein aggregates are detected at the subcellular level, along the neurites and strikingly, in dendritic spines, which has not been possible until now. Here, a polymorphic nature of amyloid structures that exist in AD transgenic neurons is reported. Based on the findings of this work, it is suggested that structural polymorphism of amyloid proteins that occur already in neurons may trigger different mechanisms of AD progression.

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Section: Introductionmentioning

confidence: 99%

Super‐Resolution Infrared Imaging of Polymorphic Amyloid Aggregates Directly in Neurons

et al. 2020

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“…In order to inquire the presence of possible correlations among the secondary structures of the samples, we analyzed the experimental data through a PCA model, an approach that has been extensively used to classify calculated structures in proteins 61 , identify spectroscopic markers 29,48,62 , and determine protein dynamics 63 . The model uses as variables the percentage amount of the structures obtained by the deconvolution/fitting of the µ-FTIR reflectance spectra (all the 12 different secondary structures), plus the samples age, for 50 silk samples (Mod, Mod1-2, HS1-47).…”

Section: Resultsmentioning

confidence: 99%

Understanding the structural degradation of South American historical silk: A Focal Plane Array (FPA) FTIR and multivariate analysis

Badillo-Sanchez

Chelazzi

Giorgi

et al. 2019

Sci Rep

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Silk artifacts constitute an invaluable heritage, and to preserve such patrimony it is necessary to correlate the degradation of silk fibroin with the presence of dyes, pollutants, manufacturing techniques, etc. Fourier Transform Infrared Spectroscopy with a Focal plane array detector (FPA FTIR) provides structural information at the micron scale. We characterized the distribution of secondary structures in silk fibers for a large set of South American historical textiles, coupling FTIR with multivariate statistical analysis to correlate the protein structure with the age of the samples and the presence of dyes. We found that the pressure applied during attenuated total reflectance (ATR) measurements might induce structural changes in the fibers, producing similar spectra for pristine and aged samples. Reflectance spectra were thus used for the rigorous characterization of secondary structures. Some correlation was highlighted between the age of the samples (spanning over five centuries) and specific changes in their secondary structure. A correlation was found between the color of the samples and structural alterations, in agreement with the chemical nature of the dyes. Overall, we demonstrated the efficacy of reflectance FPA µ-FTIR, combined with multivariate analysis, for the rigorous and non-invasive description of protein secondary structures on large sets of samples.

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“…(Figure S1). In addition, when experiments at Aβ concentrations in the submicromolar regime are performed, rates of simple collision‐induced aggregation or nucleation‐dependent polymerization are so low that no substantial aggregation occurs . Figure b shows a typical SERS spectrum of Aβ42.…”

Section: Resultsmentioning

confidence: 99%

Ultrasensitive amyloid β‐protein quantification with high dynamic range using a hybrid graphene–gold surface‐enhanced Raman spectroscopy platform

Hayden

Wang

et al. 2019

J Raman Spectroscopy

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Surface enhanced Raman spectroscopy (SERS) holds great promise in biosensing because of its single‐molecule, label‐free sensitivity. We describe here the use of a graphene–gold hybrid plasmonic platform that enables quantitative SERS measurement. Quantification is enabled by normalizing analyte peak intensities to that of the graphene G peak. We show that two complementary quantification modes are intrinsic features of the platform and that through their combined use, the platform enables accurate determination of analyte concentration over a concentration range spanning seven orders of magnitude. We demonstrate, using a biologically relevant test analyte, the amyloid β‐protein (Aβ), a seminal pathologic agent of Alzheimer's disease, that linear relationships exist between (a) peak intensity and concentration at a single plasmonic hot spot smaller than 100 nm and (b) frequency of hot spots with observable protein signals, that is, the colocation of an Aβ protein and a hot spot. We demonstrate the detection of Aβ at a concentration as low as 10−18 M after a single 20 μl aliquot of the analyte onto the hybrid platform. This detection sensitivity can be improved further through multiple applications of analyte to the platform and by rastering the laser beam with smaller step sizes.

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

Cited by 39 publications

References 26 publications

Super‐Resolution Infrared Imaging of Polymorphic Amyloid Aggregates Directly in Neurons

Super‐Resolution Infrared Imaging of Polymorphic Amyloid Aggregates Directly in Neurons

Understanding the structural degradation of South American historical silk: A Focal Plane Array (FPA) FTIR and multivariate analysis

Ultrasensitive amyloid β‐protein quantification with high dynamic range using a hybrid graphene–gold surface‐enhanced Raman spectroscopy platform

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