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Analysis of Fluorescent Proteins with a Nanoparticle Probe.

ABSTRACT: This letter presents the first application of high energy, single nanoparticle probes (e.g., 520 keV Au(400) 2nm NP) in the characterization of surfaces containing fluorescent proteins (e.g., GFP variants) by their co-emitted photon, electron and secondary ion signals. NP induced protein luminescence increases with the NP incident energy, is originated by the NP impact and is transferred to the protein fluorophor via electronic energy transfer. Multi-electron emission is observed per single NP impacts and their distributions are specific to the target morphology and composition. Fragment ions of protein sub-units consisting of 2-7 amino acid peptides are observed under individual NP impacts that can be correlated to the random protein orientation relative to the impact site (e.g., outer layer or "skin" of the protein).

SUBMITTER: Fernandez-Lima FA

PROVIDER: S-EPMC3270945 | biostudies-literature | 2012 Feb

REPOSITORIES: biostudies-literature

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Analysis of Fluorescent Proteins with a Nanoparticle Probe.

Fernandez-Lima Francisco A FA Eller Michael J MJ Debord J Daniel JD Levy Michaella J MJ Verkhoturov Stanislav V SV Della-Negra Serge S Schweikert Emile A EA

The journal of physical chemistry letters 20120201 3

This letter presents the first application of high energy, single nanoparticle probes (e.g., 520 keV Au(400) 2nm NP) in the characterization of surfaces containing fluorescent proteins (e.g., GFP variants) by their co-emitted photon, electron and secondary ion signals. NP induced protein luminescence increases with the NP incident energy, is originated by the NP impact and is transferred to the protein fluorophor via electronic energy transfer. Multi-electron emission is observed per single NP i ...[more]

PMID: 22308203

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