Single Molecule Vibrational Fine-structure of Tyrosine Adsorbed on Ag Nano-Crystals

Bjerneld, Erik J.; Johansson, Patrik; Käll, Mikael

doi:10.1002/1438-5171(200009)1:3<239::aid-simo239>3.3.co;2-w

Cited by 35 publications

(85 citation statements)

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“…The strong enhancement of the band at approximately 1500 cm −1 due to the ν (C = C) mode (F19a) of the benzene ring of Tyr suggests interaction of the peptide with the Ag surface via the Tyr moiety. As shown in previous contributions, Tyr adsorbs on the Ag surface adopting almost parallel orientation versus the metal surface, which allows on the involvement in the bonding of the π‐orbitals of the benzene ring . However, small differences in this more‐or‐less horizontal arrangement of the benzene ring onto the Ag surface were observed, and they contribute to the slight variations in the wavenumber of the F19a band (1493–1506 cm −1 ).…”

Section: Resultssupporting

confidence: 74%

“…Similar enhancement of the F19a mode has been reported for l ‐Phe phosphonodipeptide analogues and substituted with phenyl fragment α ‐aminophosphinic acids . Previous investigations showed that Tyr coordinates with the Ag surface as tyrosinate, either as an anion or as a radical, in various chemisorptions states even though the phenolic hydroxyl group in Tyr exhibits a pKa of 10.07 . One can suppose that dissociation of the OH group occurs in this case.…”

Section: Resultsmentioning

confidence: 99%

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Adsorption of neurotensin‐family peptides on SERS‐active Ag substrates

Podstawka-Proniewicz

Kudelski

Kim

et al. 2012

J Raman Spectroscopy

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Kinetensin (KN) and its amino acids 1–8 fragment ([des‐Leu9]KN), neuromedin N (NMN), and xenopsin (XP) and its two analogs (XP‐1 and XP‐2) belong to the neurotensin family of peptides and are known to stimulate the growth of human tumors. In this work, we report Fourier transform‐Raman and surface‐enhanced Raman scattering (SERS) studies of these peptides and discuss their structures, orientation, and mode of adsorption onto a highly specific, electrochemically roughened SERS‐active Ag electrode that is characterized by the formation of a 50–150 nm Ag island on its surface. We show that the investigated peptides bind preferentially to this surface by substantial electronic overlap between the metal surface and the π‐orbitals of the benzene rings of the Phe, Tyr, and Trp residues, which forces them to take parallel or almost parallel orientations with respect to the surface. In addition, the –CH2–, –CNH2, and –COO‐ molecular fragments are involved in interactions with (binding to or in close proximity with) the Ag surface. The SERS data show that the adsorption modes in each of these cases are very similar. In addition, we show that the specific differences in the amino acid sequences do not significantly affect the orientation of the investigated peptides on the Ag substrate. This result implies that the N‐termini of the neurotensin‐family peptides do not influence the mode for adsorption onto the Ag substrates. Copyright © 2012 John Wiley & Sons, Ltd.

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Section: Resultssupporting

confidence: 74%

Section: Resultsmentioning

confidence: 99%

Adsorption of neurotensin‐family peptides on SERS‐active Ag substrates

Podstawka-Proniewicz

Kudelski

Kim

et al. 2012

J Raman Spectroscopy

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“…However, when phenoxyl oxygen is a strong hydrogen‐bond acceptor, the relative intensity ratio of the Fermi doublet increases to 2.5, whereas an I 850 /I 830 ratio between 1 and 1.4 indicates that the phenolic group plays the role of a donor and acceptor of moderate H‐bonds. In the absence of hydrogen bonding, the relative intensity of the 850 cm ‐1 band is greatly enhanced . As previously mentioned, the I 850 /I 830 ratio increased from 1.3 for native C ‐terminal fragments (NT 9‐13 and NT 8‐13 ) adsorbed on the colloidal silver surface to 2.5 for NMN, which suggests the lack of the Tyr hydrogen bonding (Tyr‐O ‐ turned to the silver surface) upon natural modification of the NT 8‐13 fragment.…”

Section: Resultssupporting

confidence: 90%

Adsorption mode of neurotensin family peptides onto a colloidal silver surface: SERS studies

Proniewicz

Ozaki

Kim

et al. 2012

J Raman Spectroscopy

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Kinetensin (KN) and its amino acids 1–8 fragment ([des‐Leu9]KN), neuromedin N (NMN), and xenopsin (XP) and its two analogs (human XP‐1/xenin‐8 and XP‐2) belong to the neurotensin family of peptides and are known to stimulate the growth of human tumors. In this work, we report surface‐enhanced Raman scattering (SERS) studies of these peptides and discuss their structures, orientation, and mode of adsorption onto a colloidal assembly of apparently randomly adhering Ag spheres with diameters of approximately 20 – 25 nm. We show that small alternations in both the amino acid composition and tertiary structure, which induce striking biological in vitro, were responsible for the observed spectroscopic changes. Copyright © 2012 John Wiley & Sons, Ltd.

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“…This has become a pressing issue in the last decade, when TERS was applied for nanoscale spectroscopic imaging of native protein assemblies, ( Figure A). The photochemical degradation of the analyte leads to missing spectral features, large fluctuations in the spectra and lack of resemblance to the bulk Raman spectra of the same molecules . In particular, the amide I band (which is the clearest Raman marker of peptide bonds) is frequently missing in the SER/TER spectra of proteins and peptides (Figure B, see detailed discussion in Section S1, Supporting Information).…”

Section: Introductionmentioning

confidence: 99%

How Peptides Dissociate in Plasmonic Hot Spots

Szczerbiński

Metternich

Goubert

et al. 2020

Small

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Plasmon‐induced hot carriers enable dissociation of strong chemical bonds by visible light. This unusual chemistry has been demonstrated for several diatomic and small organic molecules. Here, the scope of plasmon‐driven photochemistry is extended to biomolecules and the reactivity of proteins and peptides in plasmonic hot spots is described. Tip‐enhanced Raman spectroscopy (TERS) is used to both drive the reactions and to monitor their products. Peptide backbone bonds are found to dissociate in the hot spot, which is reflected in the disappearance of the amide I band in the TER spectra. The observed fragmentation pathway involves nonthermal activation, presumably by dissociative capture of a plasmon‐induced hot electron. This fragmentation pathway is known from electron transfer dissociation (ETD) of peptides in gas‐phase mass spectrometry (MS), which suggests a general similarity between plasmon‐induced photochemistry and nonergodic reactions triggered by electron capture. This analogy may serve as a design principle for plasmon‐induced reactions of biomolecules.

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Single Molecule Vibrational Fine-structure of Tyrosine Adsorbed on Ag Nano-Crystals

Cited by 35 publications

References 0 publications

Adsorption of neurotensin‐family peptides on SERS‐active Ag substrates

Adsorption of neurotensin‐family peptides on SERS‐active Ag substrates

Adsorption mode of neurotensin family peptides onto a colloidal silver surface: SERS studies

How Peptides Dissociate in Plasmonic Hot Spots

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