Spatial resolution in Raman spectroscopy

Deckert, Volker; Deckert‐Gaudig, Tanja; Diegel, M.; Götz, Isabell; Langelüddecke, Lucas; Schneidewind, H.; Sharma, Gaurav; Singh, Prabha; Trautmann, Steffen; Zeisberger, Matthias; Zhang, Zhenglong

doi:10.1039/c5fd90014j

Cited by 44 publications

(37 citation statements)

References 49 publications

(56 reference statements)

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“…Next, the tip is positioned in the area of interest, and TERS spectra are point-wise collected along the selected area. The spatial resolution of TERS has been recently demonstrated to reach a few nanometers for fibrillar biological samples,[10, 14] subnanometer range and even single molecules under certain experimental conditions. [27, 28] This allows for highly resolved structural maps to be obtained with TERS for biological samples including amyloid fibrils.…”

Section: Resultsmentioning

confidence: 99%

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Polymorphism of amyloid fibrils formed by a peptide from the yeast prion protein Sup35: AFM and Tip-Enhanced Raman Scattering studies

et al. 2016

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Aggregation of prion proteins is the cause of various prion related diseases. The infectious form of prions, amyloid fibrils, exist as multiple strains. The strains are thought to represent structurally different prion protein molecules packed into amyloid fibrils, but the knowledge on the structure of different types of aggregates is limited. Here we report on the use of AFM (Atomic Force Microscopy) and TERS (Tip-Enhanced Raman Scattering) to study morphological heterogeneity and access underlying conformational features of individual amyloid aggregates. Using AFM we identified morphology of amyloid fibrils formed by the peptide (CGNNQQNY) from the yeast prion protein Sup35 that is critically involved in the aggregation of the full protein. TERS results demonstrate that morphologically different amyloid fibrils are composed of a distinct set of conformations. Fibrils formed at pH 5.6 are composed of a mixture of peptide conformations (β-sheets, random coil and α-helix) while fibrils formed in pH~2 solution primarily have β-sheets. Additionally, peak positions in the amide III region of the TERS spectra suggested that peptides have parallel arrangement of β-sheets for pH~2 fibrils and antiparallel arrangement for fibrils formed at pH 5.6. We also developed a methodology for detailed analysis of the peptide secondary structure by correlating intensity changes of Raman bands in different regions of TERS spectra. Such correlation established that structural composition of peptides is highly localized with large contribution of unordered secondary structures on a fibrillar surface.

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Section: Resultsmentioning

confidence: 99%

“…[10, 13] These studies demonstrated the potential of TERS to assess structural characteristics of amyloid fibril with high lateral resolution. [14]…”

Section: Introductionmentioning

confidence: 99%

Polymorphism of amyloid fibrils formed by a peptide from the yeast prion protein Sup35: AFM and Tip-Enhanced Raman Scattering studies

et al. 2016

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“…92,104 The origin of these band fluctuations is not yet clear. It was proposed that such band shifts could be due to molecule-metal interactions and incident light polarization.…”

Section: Polarized Raman Spectroscopy Of Insulin Fibrilsmentioning

confidence: 98%

Exploring the structure and formation mechanism of amyloid fibrils by Raman spectroscopy: a review

Kurouski

Duyne

Lednev

2015

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Amyloid fibrils are β-sheet rich protein aggregates that are strongly associated with various neurodegenerative diseases. Raman spectroscopy has been broadly utilized to investigate protein aggregation and amyloid fibril formation and has been shown to be capable of revealing changes in secondary and tertiary structures at all stages of fibrillation. When coupled with atomic force (AFM) and scanning electron (SEM) microscopies, Raman spectroscopy becomes a powerful spectroscopic approach that can investigate the structural organization of amyloid fibril polymorphs. In this review, we discuss the applications of Raman spectroscopy, a unique, label-free and non-destructive technique for the structural characterization of amyloidogenic proteins, prefibrilar oligomers, and mature fibrils.

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“…We demonstrate ac ombination of conventionalR aman spectroscopy and tip-enhanced Ramans pectroscopy (TERS) for resolving morphological and structurald ifferenceso fd ifferently prepared hexolite nanocomposites. [11][12][13] The TERS experiment provides access to both the topography and chemical composition in as ingle experiment. [1,2] Recent progress allowed for af urtherd ecrease in the size of synthetic nanodiamonds via TNT (2,4,6-trinitrotoluene)-RDX (1,3,5-trinitro-1,3,5-triazine) or TNT-HMX( octahydro-1,3,5,7-tetranitro-1,3,5,7-tetrazocine) mixtureso btained in the spray flash evaporation (SFE) process.…”

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confidence: 99%

“…To understandt he underlying mechanism,t he chemical composition of the nanomaterial must be investigated. [11][12][13] The TERS experiment provides access to both the topography and chemical composition in as ingle experiment. TNT and RDX were either mixed after separatec rystallization (hexolite-1), or the components were mixed prior to the crystallization process (hexolite-2).…”

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High‐resolution Raman Spectroscopy for the Nanostructural Characterization of Explosive Nanodiamond Precursors

et al. 2016

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The specific attributes of nanodiamonds have attracted increasing interest for electronics or biomedical applications. An efficient synthetic route towards nanodiamonds is via detonation of hexolite (i.e. a mixture of TNT [2,4,6-trinitrotoluene] and RDX [1,3,5-trinitro-1,3,5-triazine]). In particular, detonation of hexolite crystallized by spray flash evaporation (SFE) yields extremely small diamonds (<4 nm). To unravel the detonation mechanism, a structural characterization of the explosives is required but is challenging due to their thermal instability. We demonstrate a combination of conventional Raman spectroscopy and tip-enhanced Raman spectroscopy (TERS) for resolving morphological and structural differences of differently prepared hexolite nanocomposites. The experiments allow for the first time a structural differentiation of individual TNT and RDX crystals and 15-20 nm sized core-shell structures, consequently providing a general approach to investigate the actual composition of mixtures on the nanometer scale.

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Spatial resolution in Raman spectroscopy

Abstract: This article is intended to set the scope of the meeting, in particular, the high spatial resolution section.

Cited by 44 publications

References 49 publications

Polymorphism of amyloid fibrils formed by a peptide from the yeast prion protein Sup35: AFM and Tip-Enhanced Raman Scattering studies

Polymorphism of amyloid fibrils formed by a peptide from the yeast prion protein Sup35: AFM and Tip-Enhanced Raman Scattering studies

Exploring the structure and formation mechanism of amyloid fibrils by Raman spectroscopy: a review

High‐resolution Raman Spectroscopy for the Nanostructural Characterization of Explosive Nanodiamond Precursors

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