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How Peptides Dissociate in Plasmonic Hot Spots
Author(s) -
Szczerbiński Jacek,
Metternich Jonas B.,
Goubert Guillaume,
Zenobi Renato
Publication year - 2020
Publication title -
small
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.785
H-Index - 236
eISSN - 1613-6829
pISSN - 1613-6810
DOI - 10.1002/smll.201905197
Subject(s) - plasmon , electron transfer dissociation , biomolecule , photochemistry , chemistry , dissociation (chemistry) , mass spectrometry , molecule , fragmentation (computing) , raman spectroscopy , infrared multiphoton dissociation , tandem mass spectrometry , materials science , organic chemistry , optoelectronics , biochemistry , physics , chromatography , computer science , optics , operating system
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.