Understanding the nanoparticle-protein corona using methods to quantify exchange rates and affinities of proteins for nanoparticles
(2007) In Proceedings of the National Academy of Sciences 104(7). p.2050-2055- Abstract
- Due to their small size, nanoparticles have distinct properties compared with the bulk form of the same materials. These properties are rapidly revolutionizing many areas of medicine and technology. Despite the remarkable speed of development of nanoscience, relatively little is known about the interaction of nanoscale objects with living systems. In a biological fluid, proteins associate with nanoparticles, and the amount and presentation of the proteins on the surface of the particles leads to an in vivo response. Proteins compete for the nanoparticle "surface," leading to a protein "corona" that largely defines the biological identity of the particle. Thus, knowledge of rates, affinities, and stoichiometries of protein association with,... (More)
- Due to their small size, nanoparticles have distinct properties compared with the bulk form of the same materials. These properties are rapidly revolutionizing many areas of medicine and technology. Despite the remarkable speed of development of nanoscience, relatively little is known about the interaction of nanoscale objects with living systems. In a biological fluid, proteins associate with nanoparticles, and the amount and presentation of the proteins on the surface of the particles leads to an in vivo response. Proteins compete for the nanoparticle "surface," leading to a protein "corona" that largely defines the biological identity of the particle. Thus, knowledge of rates, affinities, and stoichiometries of protein association with, and dissociation from, nanoparticles is important for understanding the nature of the particle surface seen by the functional machinery of cells. Here we develop approaches to study these parameters and apply them to plasma and simple model systems, albumin and fibrinogen. A series of copolymer nanoparticles are used with variation of size and composition (hydrophobicity). We show that isothermal titration calorimetry is suitable for studying the affinity and stoichiometry of protein binding to nanoparticles. We determine the rates of protein association and dissociation using surface plasmon resonance technology with nanoparticles that are thiol-linked to gold, and through size exclusion chromatography of protein-nanoparticle mixtures. This method is less perturbing than centrifugation, and is developed into a systematic methodology to isolate nanoparticle-associated proteins. The kinetic and equilibrium binding properties depend on protein identity as well as particle surface characteristics and size. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/672947
- author
- Cedervall, Tommy LU ; Lynch, Iseult ; Lindman, Stina ; Berggård, Tord LU ; Thulin, Eva ; Nilsson, Hanna ; Dawson, Kenneth A. and Linse, Sara LU
- organization
- publishing date
- 2007
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Proceedings of the National Academy of Sciences
- volume
- 104
- issue
- 7
- pages
- 2050 - 2055
- publisher
- National Academy of Sciences
- external identifiers
-
- wos:000244438500006
- scopus:33847789142
- ISSN
- 1091-6490
- DOI
- 10.1073/pnas.0608582104
- language
- English
- LU publication?
- yes
- id
- f8c4a918-0306-40b2-8d8f-2cc1fa90c7ee (old id 672947)
- date added to LUP
- 2016-04-01 11:41:44
- date last changed
- 2022-04-28 18:17:09
@article{f8c4a918-0306-40b2-8d8f-2cc1fa90c7ee,
abstract = {{Due to their small size, nanoparticles have distinct properties compared with the bulk form of the same materials. These properties are rapidly revolutionizing many areas of medicine and technology. Despite the remarkable speed of development of nanoscience, relatively little is known about the interaction of nanoscale objects with living systems. In a biological fluid, proteins associate with nanoparticles, and the amount and presentation of the proteins on the surface of the particles leads to an in vivo response. Proteins compete for the nanoparticle "surface," leading to a protein "corona" that largely defines the biological identity of the particle. Thus, knowledge of rates, affinities, and stoichiometries of protein association with, and dissociation from, nanoparticles is important for understanding the nature of the particle surface seen by the functional machinery of cells. Here we develop approaches to study these parameters and apply them to plasma and simple model systems, albumin and fibrinogen. A series of copolymer nanoparticles are used with variation of size and composition (hydrophobicity). We show that isothermal titration calorimetry is suitable for studying the affinity and stoichiometry of protein binding to nanoparticles. We determine the rates of protein association and dissociation using surface plasmon resonance technology with nanoparticles that are thiol-linked to gold, and through size exclusion chromatography of protein-nanoparticle mixtures. This method is less perturbing than centrifugation, and is developed into a systematic methodology to isolate nanoparticle-associated proteins. The kinetic and equilibrium binding properties depend on protein identity as well as particle surface characteristics and size.}},
author = {{Cedervall, Tommy and Lynch, Iseult and Lindman, Stina and Berggård, Tord and Thulin, Eva and Nilsson, Hanna and Dawson, Kenneth A. and Linse, Sara}},
issn = {{1091-6490}},
language = {{eng}},
number = {{7}},
pages = {{2050--2055}},
publisher = {{National Academy of Sciences}},
series = {{Proceedings of the National Academy of Sciences}},
title = {{Understanding the nanoparticle-protein corona using methods to quantify exchange rates and affinities of proteins for nanoparticles}},
url = {{http://dx.doi.org/10.1073/pnas.0608582104}},
doi = {{10.1073/pnas.0608582104}},
volume = {{104}},
year = {{2007}},
}