Chemische Bildgebung auf der Nanometerskala mittels spitzenverstärkter Raman‐Spektroskopie

Schmid, Thomas; Opilik, Lothar; Blum, Carolin; Zenobi, Renato

doi:10.1002/ange.201203849

Cited by 20 publications

(1 citation statement)

References 133 publications

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“…It is mainly caused by two factors: the first factor is not fully understood, but the observed unspecific broad background is often explained by a plasmon-dependent photoluminesence of the rough metal surface (or the tip−sample gap). 16,17 Second, the enhanced and confined electromagnetic field in direct proximity to the tip can cause sample degradation. 3 For long measurement times (in the range of minutes) as used in this study, the Raman signals of the resulting carbonaceous species average to two broad bands centered around 1350 and 1580 cm −1 .…”

Section: ■ Results and Discussionmentioning

confidence: 99%

Missing Amide I Mode in Gap-Mode Tip-Enhanced Raman Spectra of Proteins

et al. 2012

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Tip-enhanced Raman spectroscopy is a surface sensitive analytical method that combines the advantages of scanning probe microscopy and Raman spectroscopy. It holds great promises for imaging of biological samples with high spatial resolution (10−50 nm), well below the optical diffraction limit. It offers the opportunity to directly localize and identify proteins and their conformation in a complex (e.g., native) environment. Tip-enhanced Raman (TER) spectra in the socalled "gap-mode" configuration with a metal tip in scanning tunnelling feedback with a metal substrate coated with different proteins (bovine serum albumin, immunoglobulin G, trypsin, and β-lactoglobulin) as well as of model octapeptides (with and without an aromatic amino acid residue) are presented. The goal was to determine if it is possible to reliably assign marker bands for proteins and if different secondary structures of proteins can be distinguished in their gap-mode TER spectra as reliably as by IR and conventional Raman spectroscopy. It is shown that contrary to the presented conventional Raman spectra of proteins the amide I mode, which is widely used to identify secondary structure motifs of proteins, is not visible in gap-mode TERS. Aromatic modes are prominent and can be used as reliable marker bands for imaging of proteins in a complex environment.

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Section: ■ Results and Discussionmentioning

confidence: 99%

Missing Amide I Mode in Gap-Mode Tip-Enhanced Raman Spectra of Proteins

et al. 2012

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Thomson‐Medaille: C. V. Robinson und R. Zenobi / SGMS‐Preis: Y. O. Tsybin / Verdienstkreuz am Bande des Verdienstordens der Bundesrepublik Deutschland: G. Erker / Theodor‐Förster‐Gedächtnisvorlesung: B. L. Feringa

2014

Angewandte Chemie

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Chirality‐Assisted Ring‐Like Aggregation of Aβ(1–40) at Liquid–Solid Interfaces: A Stereoselective Two‐Step Assembly Process

et al. 2014

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Molecular chirality is introduced at liquid–solid interfaces. A ring‐like aggregation of amyloid Aβ(1–40) on N‐isobutyryl‐L‐cysteine (L‐NIBC)‐modified gold substrate occurs at low Aβ(1–40) concentration, while D‐NIBC modification only results in rod‐like aggregation. Utilizing atomic force microscope controlled tip‐enhanced Raman scattering, we directly observe the secondary structure information for Aβ(1–40) assembly in situ at the nanoscale. D‐ or L‐NIBC on the surface can guide parallel or nonparallel alignment of β‐hairpins through a two‐step process based on electrostatic‐interaction‐enhanced adsorption and subsequent stereoselective recognition. Possible electrostatic interaction sites (R5 and K16) and a chiral recognition site (H14) of Aβ(1–40) are proposed, which may provide insight into the understanding of this effect.

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Chemische Bildgebung auf der Nanometerskala mittels spitzenverstärkter Raman‐Spektroskopie

Cited by 20 publications

References 133 publications

Missing Amide I Mode in Gap-Mode Tip-Enhanced Raman Spectra of Proteins

Missing Amide I Mode in Gap-Mode Tip-Enhanced Raman Spectra of Proteins

Thomson‐Medaille: C. V. Robinson und R. Zenobi / SGMS‐Preis: Y. O. Tsybin / Verdienstkreuz am Bande des Verdienstordens der Bundesrepublik Deutschland: G. Erker / Theodor‐Förster‐Gedächtnisvorlesung: B. L. Feringa

Chirality‐Assisted Ring‐Like Aggregation of Aβ(1–40) at Liquid–Solid Interfaces: A Stereoselective Two‐Step Assembly Process

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