Publication

Mapping protein binding sites on the biomolecular corona of nanoparticles

Kelly, P. M., Åberg, C., Polo, E., O'Connell, A., Cookman, J., Fallon, J., Krpetić, Ž. & Dawson, K. A., 2015, In : Nature Nanotechnology. 10, 5, p. 472-479

Research output: Contribution to journalArticleAcademicpeer-review

  • Philip M. Kelly
  • Christoffer Åberg
  • Ester Polo
  • Ann O'Connell
  • Jennifer Cookman
  • Jonathan Fallon
  • Željka Krpetić
  • Kenneth A. Dawson
Nanoparticles in a biological milieu are known to form a sufficiently long-lived and well-organized ‘corona’ of biomolecules to confer a biological identity to the particle. Because this nanoparticle–biomolecule complex interacts with cells and biological barriers, potentially engaging with different biological pathways, it is important to clarify the presentation of functional biomolecular motifs at its interface. Here, we demonstrate that by using antibody-labelled gold nanoparticles, differential centrifugal sedimentation and various imaging techniques it is possible to identify the spatial location of proteins, their functional motifs and their binding sites. We show that for transferrin-coated polystyrene nanoparticles only a minority of adsorbed proteins exhibit functional motifs and the spatial organization appears random, which is consistent, overall, with a stochastic and irreversible adsorption process. Our methods are applicable to a wide array of nanoparticles and can offer a microscopic molecular description of the biological identity of nanoparticles.
Original languageEnglish
Pages (from-to)472-479
JournalNature Nanotechnology
Volume10
Issue number5
Early online date30-Mar-2015
Publication statusPublished - 2015
Externally publishedYes

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