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Mapping and identification of soft corona proteins at nanoparticles and their impact on cellular association
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Abstract
The current understanding of the biological identity that nanoparticles may acquire in a given biological milieu is mostly inferred from the hard component of the protein corona (HC). The composition of soft corona (SC) proteins and their biological relevance have remained elusive due to the lack of analytical separation methods. Here, we identify a set of specific corona proteins with weak interactions at silica and polystyrene nanoparticles by using an in situ click-chemistry reaction. We show that these SC proteins are present also in the HC, but are specifically enriched after the capture, suggesting that the main distinction between HC and SC is the differential binding strength of the same proteins. Interestingly, the weakly interacting proteins are revealed as modulators of nanoparticle-cell association mainly through their dynamic nature. We therefore highlight that weak interactions of proteins at nanoparticles should be considered when evaluating nano-bio interfaces.
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Cites
Double-slit photoelectron interference in strong-field ionization of the neon dimer
Kunitski, M., Eicke, N., Huber, P., Köhler, J., Zeller, S., Voigtsberger, J., Schlott, N., Henrichs, K., Sann, H., Trinter, F., et al. (2019) · Nature Communications · doi:10.1038/s41467-018-07882-8 · Cited by 8,162
Erickson, H. P. (2009) · Biological Procedures Online · doi:10.1007/s12575-009-9008-x · Cited by 1,571
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
Treuel, L., Brandholt, S., Maffre, P., Wiegele, S., Shang, L., & Nienhaus, G. U. (2014) · ACS Nano · doi:10.1021/nn405019v · Cited by 419
The viral protein corona directs viral pathogenesis and amyloid aggregation
Ezzat, K., Pernemalm, M., Pålsson, S., Roberts, T. C., Järver, P., Dondalska, A., Bestas, B., Sobkowiak, M. J., Levänen, B., Sköld, M., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-10192-2 · Cited by 209
Research works printed but not linked: 53
- Wang, H. et al. The nature of a hard protein corona forming on quantum dots exposed to human blood serum. Small 12, 5836–5844 (2016). · DOI
- Digiacomo, L., Giulimondi, F., Mahmoudi, M. & Caracciolo, G. Effect of molecular crowding on the biological identity of liposomes: an overlooked factor at the bio-nano interface. Nanoscale Adv. 1, 2518–2522 (2019). · DOI
- Hayashi, Y. et al. Species differences take shape at nanoparticles: protein corona made of the native repertoire assists cellular interaction. Envir. Sci. Tech. 47, 14367–14375 (2013). · DOI
- Monopoli, M. P., Åberg, C., Salvati, A. & Dawson, K. A. Biomolecular coronas provide the biological identity of nanosized materials. Nat. Nanotechnol. 7, 779–786 (2012). · DOI · Paper page
- Berardi, A. & Baldelli Bombelli, F. Oral delivery of nanoparticles-let’s not forget about the protein corona. Expert Opin. Drug Del. 16, 563–566 (2019). · DOI
- Weiss, A. C. et al. Link between low-fouling and stealth: a whole blood biomolecular corona and cellular association analysis on nanoengineered particles. ACS Nano 13, 4980–4991 (2019). · DOI
- Francia, V. et al. Corona composition can affect the mechanisms cells use to internalize nanoparticles. ACS Nano 13, 11107–11121 (2019). · DOI · Paper page
- Giulimondi, F. et al. Interplay of protein corona and immune cells controls blood residency of liposomes. Nat. Commun. 10, 1–11 (2019). · DOI · Paper page
- Vu, V. P. et al. Immunoglobulin deposition on biomolecule corona determines complement opsonization efficiency of preclinical and clinical nanoparticles. Nat. Nanotechnol. 14, 260 (2019). · DOI · Paper page
- Capjak, I., Goreta, S. S., Jurasin, D. D. & Vrcek, I. V. How protein coronas determine the fate of engineered nanoparticles in biological environment. Arh. Hig. Rada Toksikol. 68, 245–253 (2017). · DOI
- Lesniak, A. et al. Effects of the presence or absence of a protein corona on silica nanoparticle uptake and impact on cells. ACS Nano 6, 5845–5857 (2012). · DOI · Paper page
- Vroman, L. & Adams, A. L. Identification of rapid changes at plasma-solid interfaces. J. Biomed. Mater. Res. 3, 43–67 (1969). · DOI · Paper page
- Llopis-Lorente, A. et al. Enzyme-powered gated mesoporous silica nanomotors for on-command intracellular payload delivery. ACS Nano 13, 12171–12183 (2019). · DOI
- Cedervall, T. et al. Understanding the nanoparticle-protein corona using methods to quantify exchange rates and affinities of proteins for nanoparticles. Proc. Natl Acad. Sci. USA 104, 2050–2055 (2007). · DOI · Paper page
- Patel, H. Serum opsonins and liposomes: their interaction and opsonophagocytosis. Crit. Rev. Ther. Drug 9, 39–90 (1992).
- Micluas, T. et al. Dynamic protein coronas revealed as a modulator of silver nanoparticle sulphidation in vitro. Nat. Commun. 7, 11770 (2016). · DOI · Paper page
- Fleischer, C. C. & Payne, C. K. Secondary structure of corona proteins determines the cell surface receptors used by nanoparticles. J. Phys. Chem. B 118, 14017–14026 (2014). · DOI · Paper page
- Wang, J. et al. Soft interactions at nanoparticles alter protein function and conformation in a size dependent manner. Nano Lett. 11, 4985–4991 (2011). · DOI · Paper page
- Miclaus, T., Bochenkov, V. E., Ogaki, R., Howard, K. A. & Sutherland, D. S. Spatial mapping and quantification of soft and hard protein coronas at silver nanocubes. Nano Lett. 14, 2086–2093 (2014). · DOI
- Weiss, A. C. et al. In situ characterization of protein corona formation on silica microparticles using confocal laser scanning microscopy combined with microfluidics. ACS Appl. Mater. Inter. 11, 2459–2469 (2019). · DOI
- Yan, Y. et al. Differential roles of the protein corona in the cellular uptake of nanoporous polymer particles by monocyte and macrophage cell lines. ACS Nano 7, 10960–10970 (2013). · DOI · Paper page
- Walczyk, D., Bombelli, F. B., Monopoli, M. P., Lynch, I. & Dawson, K. A. What the cell “sees” in bionanoscience. J. Am. Chem. Soc. 132, 5761–5768 (2010). · DOI · Paper page
- Kokkinopoulou, M., Simon, J., Landfester, K., Mailänder, V. & Lieberwirth, I. Visualization of the protein corona: towards a biomolecular understanding of nanoparticle-cell-interactions. Nanoscale 9, 8858–8870 (2017). · DOI · Paper page
- Bonvin, D., Chiappe, D., Moniatte, M., Hofmann, H. & Ebersold, M. M. Methods of protein corona isolation for magnetic nanoparticles. Analyst 142, 3805–3815 (2017). · DOI
- Weber, C., Simon, J., Mailänder, V., Morsbach, S. & Landfester, K. Preservation of the soft protein corona in distinct flow allows identification of weakly bound proteins. Acta Biomaterialia 76, 217–224 (2018). · DOI
- Kari, O. K. et al. In situ analysis of liposome hard and soft protein corona structure and composition in a single label-free workflow. Nanoscale 12, 1728–1741 (2020). · DOI
- Liu, X. et al. Rapid conjugation of nanoparticles, proteins and siRNAs to microbubbles by strain-promoted click chemistry for ultrasound imaging and drug delivery. Polym. Chem. 10, 705–717 (2019). · DOI
- DeForest, C. A. & Anseth, K. S. Cytocompatible click-based hydrogels with dynamically tunable properties through orthogonal photoconjugation and photocleavage reactions. Nat. Chem. 3, 925 (2011). · DOI · Paper page
- Ishizuka, T., Liu, H. S., Ito, K. & Xu, Y. Fluorescence imaging of chromosomal DNA using click chemistry. Sci. Rep. 6, 33217 (2016). · DOI
- Schreiber, C. L. & Smith, B. D. Molecular conjugation using non-covalent click chemistry. Nat. Rev. Chem. 3, 393–400 (2019). · DOI
- Wang, S. et al. Regulation of Ca2+ Signaling for drug‐resistant breast cancer therapy with mesoporous silica nanocapsule encapsulated doxorubicin/siRNA cocktail. ACS Nano 13, 274–283 (2018). · DOI
- Li, L. et al. Polystyrene nanoparticles reduced ROS and inhibited ferroptosis by triggering lysosome stress and TFEB nucleus translocation in a size-dependent manner. Nano Lett. 19, 7781–7792 (2019). · DOI
- Hajipour, M. J., Laurent, S., Aghaie, A., Rezaee, F. & Mahmoudi, M. Personalized protein coronas: a “key” factor at the nanobiointerface. Biomater. Sci. 2, 1210–1221 (2014). · DOI · Paper page
- Carril, M. et al. In situ detection of the protein corona in complex environments. Nat. Commun. 8, 1542 (2017). · DOI
- Zeuthen, C. M., Shahrokhtash, A. & Sutherland, D. S. Nanoparticle adsorption on antifouling polymer brushes. Langmuir 35, 14879–14889 (2019). · DOI
- Tenzer, S. et al. Rapid formation of plasma protein corona critically affects nanoparticle pathophysiology. Nat. Nanotechnol. 8, 772–781 (2013). · DOI · Paper page
- Lunov, O. et al. Differential uptake of functionalized polystyrene nanoparticles by human macrophages and a monocytic cell line. ACS Nano 5, 1657–1669 (2011). · DOI · Paper page
- Platt, N. & Gordon, S. Scavenger receptors: diverse activities and promiscuous binding of polyanionic ligands. Chem. Biol. 5, R193–R203 (1998). · DOI
- Pyzik, M. et al. The neonatal Fc receptor (FcRn): a misnomer? Front. Immunol. 10, 1540 (2019). · DOI · Paper page
- Urich, E., Lazic, S. E., Molnos, J., Wells, I. & Freskgård, P.-O. Transcriptional profiling of human brain endothelial cells reveals key properties crucial for predictive in vitro blood-brain barrier models. PLoS ONE 7, e38149 (2012). · DOI
- Ritz, S. et al. Protein corona of nanoparticles: distinct proteins regulate the cellular uptake. Biomacromolecules 16, 1311–1321 (2015). · DOI · Paper page
- Thiagarajan, P., Le, A. & Benedict, C. R. Beta(2)-glycoprotein I promotes the binding of anionic phospholipid vesicles by macrophages. Arterioscler. Thromb. Vasc. Biol. 19, 2807–2811 (1999). · DOI
- Georgieva, J. V. et al. Surface characteristics of nanoparticles determine their intracellular fate in and processing by human blood-brain barrier endothelial cells in vitro. Mol. Ther. 19, 318–325 (2011). · DOI · Paper page
- Hunter, R. J. Zeta Potential in Colloid Science: Principles and Applications 2 (Academic Press, 2013).
- Monopoli, M. P., Pitek, A. S., Lynch, I. & Dawson, K. A. In Nanomaterial Interfaces in Biology 137–155 (2013). · DOI
- Gasteiger, E. et al. ExPASy: the proteomics server for in-depth protein knowledge and analysis. Nucleic Acids Res. 31, 3784–3788 (2003). · DOI · Paper page
- Lê, S., Josse, J. & Husson, F. FactoMineR: An R package for multivariate analysis. J. Stat. Softw. 25, 1–18 (2008). · DOI · Paper page
- Ishihama, Y. et al. Exponentially modified protein abundance index (emPAI) for estimation of absolute protein amount in proteomics by the number of sequenced peptides per protein. Mol. Cell Proteom. 4, 1265–1272 (2005). · DOI · Paper page
- Vorup-Jensen, T. In Integrin and Cell Adhesion Molecules 55–71 (Springer, 2011). · DOI
- Jensen, M. R. et al. Structural basis for simvastatin competitive antagonism of complement receptor 3. J. Biol. Chem. 291, 16963–16976 (2016). · DOI
- Zhao, H., Gorshkova, I. I., Fu, G. L. & Schuck, P. A comparison of binding surfaces for SPR biosensing using an antibody-antigen system and affinity distribution analysis. Methods 59, 328–335 (2013). · DOI
- Park, E. et al. Optimized THP-1 differentiation is required for the detection of responses to weak stimuli. J. Inflamm. Res. 56, 45–50 (2007). · DOI · Paper page
- Perez-Riverol, Y. et al. The PRIDE database and related tools and resources in 2019: improving support for quantification data. Nucleic Acids Res. 47, D442–D450 (2019). · DOI · Paper page
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Nanoparticle protein corona: from structure and function to therapeutic targeting
Bashiri, G., Padilla, M. S., Swingle, K. L., Shepherd, S. J., Mitchell, M. J., & Wang, K. (2023) · Lab on a Chip · doi:10.1039/d2lc00799a · Cited by 296
Protein Corona Formation on Lipid Nanoparticles Negatively Affects the NLRP3 Inflammasome Activation
Debnath, M., Forster, J., Ramesh, A., & Kulkarni, A. (2023) · Bioconjugate Chemistry · doi:10.1021/acs.bioconjchem.3c00329 · Cited by 60
Metadata
- Authors
- Mohammad-Beigi, H., Hayashi, Y., Zeuthen, C. M., Eskandari, H., Scavenius, C., Juul-Madsen, K., Vorup-Jensen, T., Enghild, J. J., & Sutherland, D. S.
- Venue
- Nature Communications
- Published
- 2020-09-10
- Volume
- 11
- Issue
- 1
- Pages
- 4535-4535
- ISSN
- 2041-1723 (ISSN-L)
- OpenAlex
- W3083833107
- Cited by
- 218
- References
- 5
- FWCI
- 7.02
- Type
- journal article
- Language
- en
- Open access
- gold
- Licence
- creativecommons.org/licenses/by/4.0 (tdm)
- creativecommons.org/licenses/by/4.0 (vor)
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