The DOI matches its Crossref record; 6 of the 6 references it cites were found in a registry or an index.
Secondary Structure of Corona Proteins Determines the Cell Surface Receptors Used by Nanoparticles
Open accessAbstract
Nanoparticles used for biological and biomedical applications encounter a host of extracellular proteins. These proteins rapidly adsorb onto the nanoparticle surface, creating a protein corona. Poly(ethylene glycol) can reduce, but not eliminate, the nonspecific adsorption of proteins. As a result, the adsorbed proteins, rather than the nanoparticle itself, determine the cellular receptors used for binding, the internalization mechanism, the intracellular transport pathway, and the subsequent immune response. Using fluorescence microscopy and flow cytometry, we first characterize a set of polystyrene nanoparticles in which the same adsorbed protein, bovine serum albumin, leads to binding to two different cell surface receptors: native albumin receptors and scavenger receptors. Using a combination of circular dichroism spectroscopy, isothermal titration calorimetry, and fluorescence spectroscopy, we demonstrate that the secondary structure of the adsorbed bovine serum albumin protein controls the cellular receptors used by the protein-nanoparticle complexes. These results show that protein secondary structure is a key parameter in determining the cell surface receptor used by a protein-nanoparticle complex. We expect this link between protein structure and cellular outcomes will provide a molecular basis for the design of nanoparticles for use in biological and biomedical applications.
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Cites
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Time Evolution of the Nanoparticle Protein Corona
Casals, E., Pfaller, T., Duschl, A., Oostingh, G. J., & Puntes, V. (2010) · ACS Nano · doi:10.1021/nn901372t · Cited by 1,211
Spherical Nucleic Acid Nanoparticle Conjugates as an RNAi-Based Therapy for Glioblastoma
Jensen, S. A., Day, E. S., Ko, C. H., Hurley, L. A., Luciano, J. P., Kouri, F. M., Merkel, T. J., Luthi, A. J., Patel, P. C., Cutler, J. I., et al. (2013) · Science Translational Medicine · doi:10.1126/scitranslmed.3006839 · Cited by 592
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Kyriakides, T. R., Raj, A., Tseng, T. H., Xiao, H., Nguyen, R., Mohammed, F. S., Halder, S., Xu, M., Wu, M. J., Bao, S., et al. (2021) · Biomedical Materials · doi:10.1088/1748-605x/abe5fa · Cited by 389
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) · Nature Nanotechnology · doi:10.1038/nnano.2015.47 · Cited by 360
Synergistic lipid compositions for albumin receptor mediated delivery of mRNA to the liver
Miao, L., Lin, J., Huang, Y., Li, L., Delcassian, D., Ge, Y., Shi, Y., & Anderson, D. G. (2020) · Nature Communications · doi:10.1038/s41467-020-16248-y · Cited by 343
Impact of protein pre-coating on the protein corona composition and nanoparticle cellular uptake
Mirshafiee, V., Kim, R., Park, S., Mahmoudi, M., & Kraft, M. L. (2016) · Biomaterials · doi:10.1016/j.biomaterials.2015.10.019 · Cited by 316
Kokkinopoulou, M., Simon, J., Landfester, K., Mailänder, V., & Lieberwirth, I. (2017) · Nanoscale · doi:10.1039/c7nr02977b · Cited by 283
Metadata
- Authors
- Fleischer, C. C., & Payne, C. K.
- Venue
- The Journal of Physical Chemistry B
- Publisher
- American Chemical Society (ACS)
- Published
- 2014-05-09
- Volume
- 118
- Issue
- 49
- Pages
- 14017-14026
- ISSN
- 1520-5207 (ISSN-L)
- 1520-6106
- OpenAlex
- W2335577615
- Cited by
- 225
- References
- 6
- FWCI
- 7.23
- Type
- journal article
- Language
- en
- Open access
- hybrid
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