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Atomic structural details of a protein grafted onto gold nanoparticles.


ABSTRACT: The development of a methodology for the structural characterization at atomic detail of proteins conjugated to nanoparticles would be a breakthrough in nanotechnology. Solution and solid-state NMR spectroscopies are currently used to investigate molecules and peptides grafted onto nanoparticles, but the strategies used so far fall short in the application to proteins, which represent a thrilling development in theranostics. We here demonstrate the feasibility of highly-resolved multidimensional heteronuclear spectra of a large protein assembly conjugated to PEGylated gold nanoparticles. The spectra have been obtained by direct proton detection under fast MAS and allow for both a fast fingerprinting for the assessment of the preservation of the native fold and for resonance assignment. We thus demonstrate that the structural characterization and the application of the structure-based methodologies to proteins bound to gold nanoparticles is feasible and potentially extensible to other hybrid protein-nanomaterials.

SUBMITTER: Giuntini S 

PROVIDER: S-EPMC5738368 | biostudies-literature | 2017 Dec

REPOSITORIES: biostudies-literature

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Atomic structural details of a protein grafted onto gold nanoparticles.

Giuntini Stefano S   Cerofolini Linda L   Ravera Enrico E   Fragai Marco M   Luchinat Claudio C  

Scientific reports 20171220 1


The development of a methodology for the structural characterization at atomic detail of proteins conjugated to nanoparticles would be a breakthrough in nanotechnology. Solution and solid-state NMR spectroscopies are currently used to investigate molecules and peptides grafted onto nanoparticles, but the strategies used so far fall short in the application to proteins, which represent a thrilling development in theranostics. We here demonstrate the feasibility of highly-resolved multidimensional  ...[more]

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