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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. © 2020 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.


    Jacek Szczerbiński, Jonas B Metternich, Guillaume Goubert, Renato Zenobi. How Peptides Dissociate in Plasmonic Hot Spots. Small (Weinheim an der Bergstrasse, Germany). 2020 Jan;16(4):e1905197

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    PMID: 31894644

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