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Cited by 3,281Nanoparticle-Based Drug DeliveryProtein Interaction Studies and Fluorescence AnalysisPolymer Surface Interaction Studies

Understanding the nanoparticle–protein corona using methods to quantify exchange rates and affinities of proteins for nanoparticles

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Cedervall, Tommy, Lynch, Iseult, Lindman, Stina, Berggård, Tord, Thulin, Eva, Nilsson, Hanna, Dawson, Kenneth A., Linse, Sara·2007·Proceedings of the National Academy of Sciences
DOI 10.1073/pnas.0608582104PMC PMC1892985
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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.

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  • Exchangeable apolipoproteins (such as ApoA, C, and E) are found in protein coronas formed on the surface of a variety of drug delivery systems.

    “Exchangeable apolipoproteins (such as ApoA, C, and E) that can direct the transport of lipids through lymphatic and circulatory systems have been found in protein coronas formed on the surface of a variety of drug delivery systems15–17.”

    From Brain-targeted drug delivery by manipulating protein corona functions (2019) · cites this paper as [15]

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Authors
Cedervall, T., Lynch, I., Lindman, S., Berggård, T., Thulin, E., Nilsson, H., Dawson, K. A., & Linse, S.
Affiliations
  • University College Dublin (IE)
  • *School of Chemistry and Chemical Biology and
  • Lund University (SE)
Corresponding author
Dawson, Kenneth A.
ORCID
Venue
Proceedings of the National Academy of Sciences
Publisher
National Academy of Sciences
Published
2007-02-13
Volume
104
Issue
7
Pages
2050-2055
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
DOI
10.1073/pnas.0608582104
PMC
PMC1892985
OpenAlex
W2057910069
Cited by
3,281
References
0
Citations by year
2026: 216 · 2025: 165 · 2024: 164 · 2023: 157 · 2022: 188 · 2021: 188 · 2020: 222 · 2019: 208 · 2018: 200 · 2017: 220 · 2016: 199 · 2015: 212 · 2014: 214 · 2013: 206 · 2012: 183
FWCI
35.35
Type
journal article
Language
en
Open access
Locations
  • Proceedings of the National Academy of Sciences (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
  • Lund University Publications (Lund University) (submittedVersion)
  • University of Birmingham Research Portal (University of Birmingham) (submittedVersion)
Topics
  • Physical Sciences › Materials Science › Biomaterials › Nanoparticle-Based Drug Delivery
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Interaction Studies and Fluorescence Analysis
  • Physical Sciences › Materials Science › Surfaces, Coatings and Films › Polymer Surface Interaction Studies
Keywords
protein corona, protein binding kinetics, binding affinity, binding stoichiometry, copolymer nanoparticles, albumin, fibrinogen, isothermal titration calorimetry, surface plasmon resonance, size exclusion chromatography, gold nanoparticles, nanoparticle hydrophobicity, nanoparticle size effects, plasma proteins
MeSH terms
Albumins, Chromatography, Gel, Fibrinogen, Kinetics, Models, Biological, Particle Size, Protein Binding, Proteins, Nanoparticles, Hydrophobic and Hydrophilic Interactions

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