Cited by 1,758Nanoparticle-Based Drug DeliveryProtein Interaction Studies and Fluorescence AnalysisNanotechnology research and applications

Understanding and controlling the interaction of nanomaterials with proteins in a physiological environment

Walkey, Carl D., Chan, Warren C. W.·2012·Chem. Soc. Rev.

Abstract

Nanomaterials hold promise as multifunctional diagnostic and therapeutic agents. However, the effective application of nanomaterials is hampered by limited understanding and control over their interactions with complex biological systems. When a nanomaterial enters a physiological environment, it rapidly adsorbs proteins forming what is known as the protein 'corona'. The protein corona alters the size and interfacial composition of a nanomaterial, giving it a biological identity that is distinct from its synthetic identity. The biological identity determines the physiological response including signalling, kinetics, transport, accumulation, and toxicity. The structure and composition of the protein corona depends on the synthetic identity of the nanomaterial (size, shape, and composition), the nature of the physiological environment (blood, interstitial fluid, cell cytoplasm, etc.), and the duration of exposure. In this critical review, we discuss the formation of the protein corona, its structure and composition, and its influence on the physiological response. We also present an 'adsorbome' of 125 plasma proteins that are known to associate with nanomaterials. We further describe how the protein corona is related to the synthetic identity of a nanomaterial, and highlight efforts to control protein-nanomaterial interactions. We conclude by discussing gaps in the understanding of protein-nanomaterial interactions along with strategies to fill them (167 references).

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Crossref · 10.1039/c1cs15233e

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  • The functionalized NPs possess unique advantages over antibody-based platforms: comparable size and diffusion kinetics to proteins, high surface area per volume and high number of flexible binding sites, and inexpensive, simple, fast, scalable synthesis with minimal batch-to-batch variability.

    “These results highlight the unique advantages that these functionalized NPs possess for protein enrichment over antibody-based platforms: (a) comparable size and diffusion kinetics to proteins, promoting effective capture of low-abundance proteins within complex mixtures20,47,48; (b) high surface area per volume and high number of flexible binding sites, contributing to high ligand density and”

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Authors
Walkey, C. D., & Chan, W. C. W.
Affiliations
University of Toronto (CA)
Corresponding author
Chan, Warren C. W.
Venue
Chem. Soc. Rev.
Published
2012
Volume
41
Issue
7
Pages
2780-2799
ISSN
  • 0306-0012 (ISSN-L)
  • 1460-4744
OpenAlex
W2050886209
Cited by
1,758
References
165
Citations by year
2026: 146 · 2025: 83 · 2024: 94 · 2023: 120 · 2022: 114 · 2021: 129 · 2020: 162 · 2019: 144 · 2018: 135 · 2017: 121 · 2016: 138 · 2015: 138 · 2014: 124 · 2013: 75 · 2012: 31
FWCI
4.41
Type
journal article
Language
en
Open access
closed
Locations
  • Chemical Society Reviews (publishedVersion)
  • PubMed (publishedVersion)
Funders
Canadian Institutes of Health Research
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 › Engineering › Biomedical Engineering › Nanotechnology research and applications
Keywords
protein corona, nanomaterial-protein interactions, plasma proteins, nanomaterial toxicity, nanomaterial design, physiological environment, interfacial composition
MeSH terms
Adsorption, Animals, Humans, Kinetics, Models, Biological, Particle Size, Proteins, Nanoparticles

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