Abstract
With the rapid developments of nanotechnology, chances of exposing nanoscale particles to humans (e.g., workers and consumers) also increase correspondingly, which raises serious concerns on their biosafety. Entrance of nanoparticles into diverse biological environment endows them with new and dynamic biological identities as the so-called nanoparticle–protein corona. Therefore, understanding the role of these nanoparticle–protein coronas and resulting biological responses is crucial, as it helps to clarify the biological mechanism and prevent the potential adverse effects of nanoparticles. In this review, we summarize the latest developments relating to the nanoparticle–protein interaction and corresponding biological responses, with an emphasis on the characterization methods, induced biological effects and possible molecular mechanisms. In addition, we overview both the challenges and opportunities (particularly in nanomedicine) raised by this entrance of nanoparticles into the living creatures, especially human beings, with some future perspectives based on our understanding.
Similar content being viewed by others
References
Alsteens D, Trabelsi H, Soumillion P, Dufrêne YF (2013) Multiparametric atomic force microscopy imaging of single bacteriophages extruding from living bacteria. Nat Commun. doi:10.1038/ncomms3926
Anderson NL, Anderson NG (2002) The human plasma proteome: history, character, and diagnostic prospects. Mol Cell Proteomics 1(11):845–867. doi:10.1074/mcp.R200007-MCP200
Babič M, Horák D, Jendelová P et al (2009) Poly(N, N-dimethylacrylamide)-coated maghemite nanoparticles for stem cell labeling. Bioconj Chem 20(2):283–294. doi:10.1021/bc800373x
Bastús NG, Sánchez-Tilló E, Pujals S et al (2009) Homogeneous conjugation of peptides onto gold nanoparticles enhances macrophage response. ACS Nano 3(6):1335–1344. doi:10.1021/nn8008273
Buijs J, Ramström M, Danfelter M, Larsericsdotter H, Håkansson P, Oscarsson S (2003) Localized changes in the structural stability of myoglobin upon adsorption onto silica particles, as studied with hydrogen/deuterium exchange mass spectrometry. J Colloid Interf Sci 263(2):441–448. doi:10.1016/S0021-9797(03)00401-6
Cai XN, Ramalingam R, Wong HS et al (2013) Characterization of carbon nanotube protein corona by using quantitative proteomics. Nanomed-Nanotechnol 9(5):583–593. doi:10.1016/j.nano.2012.09.004
Calvaresi M, Arnesano F, Bonacchi S et al (2014) C60@Lysozyme: direct observation by nuclear magnetic resonance of a 1:1 fullerene protein adduct. ACS Nano 8(2):1871–1877. doi:10.1021/nn4063374
Cedervall T, Lynch I, Lindman S et al (2007) Understanding the nanoparticle–protein corona using methods to quantify exchange rates and affinities of proteins for nanoparticles. Proc Natl Acad Sci USA 104(7):2050–2055. doi:10.1073/pnas.0608582104
Chang TY, Chang CC, Ohgami N, Yamauchi Y (2006) Cholesterol sensing, trafficking, and esterification. Annu Rev Cell Dev Biol 22:129–157. doi:10.1146/annurev.cellbio.22.010305.104656
Cho EC, Xie J, Wurm PA, Xia Y (2009) Understanding the role of surface charges in cellular adsorption versus internalization by selectively removing gold nanoparticles on the cell surface with a I2/KI etchant. Nano Lett 9(3):1080–1084
Chrousos GP (2009) Stress and disorders of the stress system. Nat Rev Endocrinol 5(7):374–381
Curtiss LK, Witztum JL (1985) Plasma apolipoproteins AI, AII, B, CI, and E are glucosylated in hyperglycemic diabetic subjects. Diabetes 34(5):452–461. doi:10.2337/diab.34.5.452
Dashti M, Kulik W, Hoek F, Veerman EC, Peppelenbosch MP, Rezaee F (2011) A phospholipidomic analysis of all defined human plasma lipoproteins. Sci Rep. http://www.nature.com/srep/2011/111107/srep00139/abs/srep00139.html#supplementary-information
Dashty M, Motazacker MM, Levels J et al (2014) Proteome of human plasma very low-density lipoprotein and low-density lipoprotein exhibits a link with coagulation and lipid metabolism. Thromb Haemost 111(3):518–530. doi:10.1160/TH13-02-0178
De Paoli SH, Diduch LL, Tegegn TZ et al (2014) The effect of protein corona composition on the interaction of carbon nanotubes with human blood platelets. Biomaterials 35(24):6182–6194. doi:10.1016/j.biomaterials.2014.04.067
Deng ZJ, Liang M, Monteiro M, Toth I, Minchin RF (2011) Nanoparticle-induced unfolding of fibrinogen promotes Mac-1 receptor activation and inflammation. Nat Nano 6(1):39–44. http://www.nature.com/nnano/journal/v6/n1/abs/nnano.2010.250.html#supplementary-information
Deng ZJ, Liang M, Toth I, Monteiro MJ, Minchin RF (2012) Molecular interaction of poly(acrylic acid) gold nanoparticles with human fibrinogen. ACS Nano 6(10):8962–8969. doi:10.1021/nn3029953
El-Sayed MA (2004) Small is different: shape-, size-, and composition-dependent properties of some colloidal semiconductor nanocrystals. Acc Chem Res 37(5):326–333. doi:10.1021/Ar020204f
Euliss LE, DuPont JA, Gratton S, DeSimone JM (2006) Imparting size, shape, and composition control of materials for nanomedicine. Chem Soc Rev 35(11):1095–1104. doi:10.1039/B600913c
Faklaris O, Joshi V, Irinopoulou T et al (2009) Photoluminescent diamond nanoparticles for cell labeling: study of the uptake mechanism in mammalian cells. ACS Nano 3(12):3955–3962
Fleischer CC, Payne CK (2014a) Nanoparticle–cell interactions: molecular structure of the protein corona and cellular outcomes. Acc Chem Res 47(8):2651–2659. doi:10.1021/ar500190q
Fleischer CC, Payne CK (2014b) Secondary structure of corona proteins determines the cell surface receptors used by nanoparticles. J Phys Chem B. doi:10.1021/jp502624n
Gaucher G, Asahina K, Wang JH, Leroux JC (2009) Effect of poly(N-vinyl-pyrrolidone)-block-poly(D, L-lactide) as coating agent on the opsonization, phagocytosis, and pharmacokinetics of biodegradable nanoparticles. Biomacromolecules 10(2):408–416. doi:10.1021/Bm801178f
Ge C, Lao F, Li W et al (2008) Quantitative analysis of metal impurities in carbon nanotubes: efficacy of different pretreatment protocols for ICPMS spectroscopy. Anal Chem 80(24):9426–9434. doi:10.1021/ac801469b
Ge C, Du J, Zhao L et al (2011a) Binding of blood proteins to carbon nanotubes reduces cytotoxicity. Proc Natl Acad Sci 108(41):16968–16973. doi:10.1073/pnas.1105270108
Ge C, Li W, Li Y et al (2011b) Significance and systematic analysis of metallic impurities of carbon nanotubes produced by different manufacturers. J Nanosci Nanotechnol 11(3):2389–2397. doi:10.1166/jnn.2011.3520
Ge C, Li Y, Yin J-J et al (2012a) The contributions of metal impurities and tube structure to the toxicity of carbon nanotube materials. NPG Asia Mater 4:e32. doi:10.1038/am.2012.60
Ge C, Meng L, Xu L et al (2012b) Acute pulmonary and moderate cardiovascular responses of spontaneously hypertensive rats after exposure to single-wall carbon nanotubes. Nanotoxicology 6(5):526–542. doi:10.3109/17435390.2011.587905
Giljohann DA, Seferos DS, Patel PC, Millstone JE, Rosi NL, Mirkin CA (2007) Oligonucleotide loading determines cellular uptake of DNA-modified gold nanoparticles. Nano Lett 7(12):3818–3821. doi:10.1021/nl072471q
Goldstein JL, Anderson RG, Brown MS (1979) Coated pits, coated vesicles, and receptor-mediated endocytosis. Nature 279(5715):679–685
Greenfield NJ (2007) Using circular dichroism spectra to estimate protein secondary structure. Nat Protoc 1(6):2876–2890. http://www.nature.com/nprot/journal/v1/n6/suppinfo/nprot.2006.202_S1.html
Gunawan C, Lim M, Marquis CP, Amal R (2014) Nanoparticle–protein corona complexes govern the biological fates and functions of nanoparticles. J Mater Chem B 2(15):2060–2083. doi:10.1039/C3TB21526A
Gupta AK, Gupta M (2005) Cytotoxicity suppression and cellular uptake enhancement of surface modified magnetic nanoparticles. Biomaterials 26(13):1565–1573. doi:10.1016/j.biomaterials.2004.05.022
Hajipour MJ, Laurent S, Aghaie A, Rezaee F, Mahmoudi M (2014) Personalized protein coronas: a “key” factor at the nanobiointerface. Biomater Sci 2(9):1210–1221. doi:10.1039/C4BM00131A
Hall CE, Slayter HS (1959) The fibrinogen molecule: its size, shape, and mode of polymerization. J Biophys Biochem Cytol 5(1):11–27. doi:10.1083/jcb.5.1.11
Helm CA, Israelachvili JN, McGuiggan PM (1989) Molecular mechanisms and forces involved in the adhesion and fusion of amphiphilic bilayers. Science 246(4932):919–922
Helm CA, Israelachvili JN, McGuiggan PM (1992) Role of hydrophobic forces in bilayer adhesion and fusion. Biochemistry 31(6):1794–1805. doi:10.1021/bi00121a030
Hu W, Peng C, Lv M et al (2011) Protein corona-mediated mitigation of cytotoxicity of graphene oxide. ACS Nano 5(5):3693–3700. doi:10.1021/nn200021j
Jiang W, KimBetty YS, Rutka JT, ChanWarren CW (2008) Nanoparticle-mediated cellular response is size-dependent. Nat Nano 3(3):145–150. http://www.nature.com/nnano/journal/v3/n3/suppinfo/nnano.2008.30_S1.html
Jiang X, Röcker C, Hafner M, Brandholt S, Dörlich RM, Nienhaus GU (2010) Endo-and exocytosis of zwitterionic quantum dot nanoparticles by live HeLa cells. ACS Nano 4(11):6787–6797
Jimenez-Cruz CA, Kang SG, Zhou RH (2014) Large scale molecular simulations of nanotoxicity. Wires Syst Biol Med 6(4):265–279. doi:10.1002/Wsbm.1271
Jin H, Heller DA, Strano MS (2008) Single-particle tracking of endocytosis and exocytosis of single-walled carbon nanotubes in NIH-3T3 cells. Nano Lett 8(6):1577–1585
Kreuter J, Hekmatara T, Dreis S, Vogel T, Gelperina S, Langer K (2007) Covalent attachment of apolipoprotein A-I and apolipoprotein B-100 to albumin nanoparticles enables drug transport into the brain. J Control Release 118(1):54–58. doi:10.1016/j.jconrel.2006.12.012
Krpetic Z, Porta F, Caneva E, Dal Santo V, Scarì G (2010) Phagocytosis of biocompatible gold nanoparticles. Langmuir 26(18):14799–14805
Laera S, Ceccone G, Rossi F et al (2011) Measuring protein structure and stability of protein–nanoparticle systems with synchrotron radiation circular dichroism. Nano Lett 11(10):4480–4484. doi:10.1021/nl202909s
Lai ZW, Yan Y, Caruso F, Nice EC (2012) Emerging techniques in proteomics for probing nano–bio interactions. ACS Nano 6(12):10438–10448. doi:10.1021/nn3052499
Laurent S, Burtea C, Thirifays C, Rezaee F, Mahmoudi M (2013a) Significance of cell “observer” and protein source in nanobiosciences. J Colloid Interf Sci 392:431–445. doi:10.1016/j.jcis.2012.10.005
Laurent S, Ng EP, Thirifays C et al (2013b) Corona protein composition and cytotoxicity evaluation of ultra-small zeolites synthesized from template free precursor suspensions. Toxicol Res 2(4):270–279. doi:10.1039/C3TX50023C
Lesniak A, Fenaroli F, Monopoli MP, Åberg C, Dawson KA, Salvati A (2012) Effects of the presence or absence of a protein corona on silica nanoparticle uptake and impact on cells. ACS Nano 6(7):5845–5857. doi:10.1021/nn300223w
Lesniak A, Salvati A, Santos-Martinez MJ, Radomski MW, Dawson KA, Åberg C (2013) Nanoparticle adhesion to the cell membrane and its effect on nanoparticle uptake efficiency. J Am Chem Soc 135(4):1438–1444. doi:10.1021/ja309812z
Limbach LK, Li Y, Grass RN et al (2005) Oxide nanoparticle uptake in human lung fibroblasts: effects of particle size, agglomeration, and diffusion at low concentrations. Environ Sci Technol 39(23):9370–9376
Lishko VK, Kudryk B, Yakubenko VP, Yee VC, Ugarova TP (2002) Regulated unmasking of the cryptic binding site for integrin αMβ2 in the γC-domain of fibrinogen†. Biochemistry 41(43):12942–12951. doi:10.1021/bi026324c
Lundqvist M (2013) Nanoparticles: tracking protein corona over time. Nat Nanotechnol 8(10):701–702. doi:10.1038/nnano.2013.196
Lundqvist M, Stigler J, Elia G, Lynch I, Cedervall T, Dawson KA (2008) Nanoparticle size and surface properties determine the protein corona with possible implications for biological impacts. Proc Natl Acad Sci USA 105(38):14265–14270. doi:10.1073/pnas.0805135105
Lunov O, Syrovets T, Loos C et al (2011) Differential uptake of functionalized polystyrene nanoparticles by human macrophages and a monocytic cell line. ACS Nano 5(3):1657–1669. doi:10.1021/nn2000756
Lynch I (2007) Are there generic mechanisms governing interactions between nanoparticles and cells? Epitope mapping the outer layer of the protein–material interface. Phys A Stat Mech Appl 373:511–520. doi:10.1016/j.physa.2006.06.008
Maiorano G, Sabella S, Sorce B et al (2010) Effects of cell culture media on the dynamic formation of protein–nanoparticle complexes and influence on the cellular response. ACS Nano 4(12):7481–7491. doi:10.1021/nn101557e
Martens S, McMahon HT (2008) Mechanisms of membrane fusion: disparate players and common principles. Nat Rev Mol Cell Biol 9(7):543–556
Mirshafiee V, Mahmoudi M, Lou K, Cheng J, Kraft ML (2013) Protein corona significantly reduces active targeting yield. Chem Commun 49(25):2557–2559. doi:10.1039/C3CC37307J
Mok H, Bae KH, Ahn C-H, Park TG (2008) PEGylated and MMP-2 specifically DePEGylated quantum dots: comparative evaluation of cellular uptake. Langmuir 25(3):1645–1650. doi:10.1021/la803542v
Monopoli MP, Walczyk D, Campbell A et al (2011) Physical–chemical aspects of protein corona: relevance to in vitro and in vivo biological impacts of nanoparticles. J Am Chem Soc 133(8):2525–2534. doi:10.1021/ja107583h
Monopoli MP, Aberg C, Salvati A, Dawson KA (2012) Biomolecular coronas provide the biological identity of nanosized materials. Nat Nano 7(12):779–786
Mortensen NP, Hurst GB, Wang W, Foster CM, Nallathamby PD, Retterer ST (2013) Dynamic development of the protein corona on silica nanoparticles: composition and role in toxicity. Nanoscale 5(14):6372–6380. doi:10.1039/C3NR33280B
Mosqueira VCF, Legrand P, Gulik A et al (2001) Relationship between complement activation, cellular uptake and surface physicochemical aspects of novel PEG-modified nanocapsules. Biomaterials 22(22):2967–2979. doi:10.1016/S0142-9612(01)00043-6
Mu Q, Jiang G, Chen L et al (2014) Chemical basis of interactions between engineered nanoparticles and biological systems. Chem Rev 114(15):7740–7781. doi:10.1021/cr400295a
Nagayama S, K-i Ogawara, Fukuoka Y, Higaki K, Kimura T (2007a) Time-dependent changes in opsonin amount associated on nanoparticles alter their hepatic uptake characteristics. Int J Pharm 342(1):215–221. doi:10.1016/j.ijpharm.2007.04.036
Nagayama S, K-i Ogawara, Minato K et al (2007b) Fetuin mediates hepatic uptake of negatively charged nanoparticles via scavenger receptor. Int J Pharm 329(1–2):192–198. doi:10.1016/j.ijpharm.2006.08.025
Pan Y, Du X, Zhao F, Xu B (2012) Magnetic nanoparticles for the manipulation of proteins and cells. Chem Soc Rev 41(7):2912–2942. doi:10.1039/c2cs15315g
Prapainop K, Witter DP, Wentworth P (2012) A chemical approach for cell-specific targeting of nanomaterials: small-molecule-initiated misfolding of nanoparticle corona proteins. J Am Chem Soc 134(9):4100–4103. doi:10.1021/ja300537u
Queiroz KCS, Tio RA, Zeebregts CJ et al (2010) Human plasma very low density lipoprotein carries Indian Hedgehog. J Proteome Res 9(11):6052–6059. doi:10.1021/pr100403q
Raemy DO, Limbach LK, Rothen-Rutishauser B et al (2011) Cerium oxide nanoparticle uptake kinetics from the gas-phase into lung cells in vitro is transport limited. Eur J Pharm and Biopharm 77(3):368–375. doi:10.1016/j.ejpb.2010.11.017
Rezaee F, Casetta B, Levels JHM, Speijer D, Meijers JCM (2006) Proteomic analysis of high-density lipoprotein. Proteomics 6(2):721–730. doi:10.1002/pmic.200500191
Rivera-Gil P, Jimenez De Aberasturi D, Wulf V et al (2012) The challenge to relate the physicochemical properties of colloidal nanoparticles to their cytotoxicity. Acc Chem Res 46(3):743–749. doi:10.1021/ar300039j
Rodahl M, Hook F, Fredriksson C et al (1997) Simultaneous frequency and dissipation factor QCM measurements of biomolecular adsorption and cell adhesion. Faraday Discuss 107:229–246
Roduner E (2006) Size matters: why nanomaterials are different. Chem Soc Rev 35(7):583–592. doi:10.1039/B502142c
Sacchetti C, Motamedchaboki K, Magrini A et al (2013) Surface polyethylene glycol conformation influences the protein corona of polyethylene glycol-modified single-walled carbon nanotubes: potential implications on biological performance. ACS Nano 7(3):1974–1989. doi:10.1021/nn400409h
Safi M, Courtois J, Seigneuret M, Conjeaud H, Berret JF (2011) The effects of aggregation and protein corona on the cellular internalization of iron oxide nanoparticles. Biomaterials 32(35):9353–9363. doi:10.1016/j.biomaterials.2011.08.048
Salvati A, Åberg C, dos Santos T et al (2011) Experimental and theoretical comparison of intracellular import of polymeric nanoparticles and small molecules: toward models of uptake kinetics. Nanomed Nanotechnol Biol Med 7(6):818–826
Salvati A, Pitek AS, Monopoli MP et al (2013) Transferrin-functionalized nanoparticles lose their targeting capabilities when a biomolecule corona adsorbs on the surface. Nat Nanotechnol 8(2):137–143
Saptarshi S, Duschl A, Lopata A (2013) Interaction of nanoparticles with proteins: relation to bio-reactivity of the nanoparticle. J Nanobiotechnol 11(1):26
Schrand AM, Lin JB, Hens SC, Hussain SM (2011) Temporal and mechanistic tracking of cellular uptake dynamics with novel surface fluorophore-bound nanodiamonds. Nanoscale 3(2):435–445
Sée V, Free P, Cesbron Y et al (2009) Cathepsin L digestion of nanobioconjugates upon endocytosis. ACS Nano 3(9):2461–2468. doi:10.1021/nn9006994
Shang L, Nienhaus K, Nienhaus G (2014) Engineered nanoparticles interacting with cells: size matters. J Nanobiotechnol 12(1):5
Sharma S, Benson HAE, Mukkur TKS, Rigby P, Chen Y (2013) Preliminary studies on the development of IgA-loaded chitosan–dextran sulphate nanoparticles as a potential nasal delivery system for protein antigens. J Microencapsul 30(3):283–294. doi:10.3109/02652048.2012.726279
Shi X, von Dem Bussche A, Hurt RH, Kane AB, Gao H (2011) Cell entry of one-dimensional nanomaterials occurs by tip recognition and rotation. Nat Nanotechnol 6(11):714–719
Shrivastava S, Nuffer JH, Siegel RW, Dordick JS (2012) Position-specific chemical modification and quantitative proteomics disclose protein orientation adsorbed on silica nanoparticles. Nano Lett 12(3):1583–1587. doi:10.1021/nl2044524
Singh S, Kumar A, Karakoti A, Seal S, Self WT (2010) Unveiling the mechanism of uptake and sub-cellular distribution of cerium oxide nanoparticles. Mol BioSyst 6(10):1813–1820
Song Y, Zhang Z, Elsayed-Ali HE et al (2011) Identification of single nanoparticles. Nanoscale 3(1):31–44. doi:10.1039/c0nr00412j
Tedja R, Lim M, Amal R, Marquis C (2012) Effects of serum adsorption on cellular uptake profile and consequent impact of titanium dioxide nanoparticles on human lung cell lines. ACS Nano 6(5):4083–4093. doi:10.1021/nn3004845
Tenzer S, Docter D, Rosfa S et al (2011) Nanoparticle size is a critical physicochemical determinant of the human blood plasma corona: a comprehensive quantitative proteomic analysis. ACS Nano 5(9):7155–7167. doi:10.1021/Nn201950e
Tenzer S, Docter D, Kuharev J et al (2013) Rapid formation of plasma protein corona critically affects nanoparticle pathophysiology. Nat Nano 8(10):772–781. doi:10.1038/nnano.2013.181
Tu Y, Lv M, Xiu P et al (2013) Destructive extraction of phospholipids from Escherichia coli membranes by graphene nanosheets. Nat Nano 8(8):594–601. doi:10.1038/nnano.2013.125
Vroman L, Adams AL, Fischer GC, Munoz PC (1980) Interaction of high molecular-weight kininogen, factor-Xii, and fibrinogen in plasma at interfaces. Blood 55(1):156–159
Wagner S, Zensi A, Wien SL, et al (2012) Uptake mechanism of apoe-modified nanoparticles on brain capillary endothelial cells as a blood–brain barrier model. Plos One. doi:10.1371/journal.pone.0032568
Walkey CD, Chan WC (2012) Understanding and controlling the interaction of nanomaterials with proteins in a physiological environment. Chem Soc Rev 41(7):2780–2799. doi:10.1039/c1cs15233e
Walkey CD, Olsen JB, Guo H, Emili A, Chan WCW (2011) Nanoparticle size and surface chemistry determine serum protein adsorption and macrophage uptake. J Am Chem Soc 134(4):2139–2147. doi:10.1021/ja2084338
Walrant A, Correia I, Jiao C-Y, et al (2011) Different membrane behaviour and cellular uptake of three basic arginine-rich peptides. Biochimica et Biophysica Acta (BBA)-Biomembr 1808(1):382–393. doi:10.1016/j.bbamem.2010.09.009
Wang F, Yu L, Monopoli MP et al (2013a) The biomolecular corona is retained during nanoparticle uptake and protects the cells from the damage induced by cationic nanoparticles until degraded in the lysosomes. Nanomed Nanotechnol Biol Med 9(8):1159–1168. doi:10.1016/j.nano.2013.04.010
Wang L, Li J, Pan J et al (2013b) Revealing the binding structure of the protein corona on gold nanorods using synchrotron radiation-based techniques: understanding the reduced damage in cell membranes. J Am Chem Soc 135(46):17359–17368. doi:10.1021/ja406924v
Whitmore L, Wallace BA (2008) Protein secondary structure analyses from circular dichroism spectroscopy: Methods and reference databases. Biopolymers 89(5):392–400. doi:10.1002/bip.20853
Wilhelm C, Gazeau F, Roger J, Pons J, Bacri J-C (2002) Interaction of anionic superparamagnetic nanoparticles with cells: kinetic analyses of membrane adsorption and subsequent internalization. Langmuir 18(21):8148–8155
Yang H, Fung S-Y, Liu M (2011) Programming the cellular uptake of physiologically stable peptide-gold nanoparticle hybrids with single amino acids. Angew Chem Int Ed 50(41):9643–9646. doi:10.1002/anie.201102911
Yuan H, Li J, Bao G, Zhang S (2010) Variable nanoparticle–cell adhesion strength regulates cellular uptake. Phys Rev Lett 105(13):138101
Zhao YL, Xing GM, Chai ZF (2008) Nanotoxicology: are carbon nanotubes safe? Nat Nanotechnol 3(4):191–192. doi:10.1038/nnano.2008.77
Zhou RH, Gao HJ (2014) Cytotoxicity of graphene: recent advances and future perspective. Wires Nanomed Nanobi 6(5):452–474. doi:10.1002/Wnan.1277
Zhu J, Zhang B, Tian J, Wang J, Chong Y, Wang X, Deng Y, Tang M, Li Y, Ge C, Pan Y, Gu H (2015) Synthesis of heterodimer radionuclide nanoparticles for magnetic resonance and single-photon emission computed tomography dual-modality imaging. Nanoscale. doi:10.1039/C4NR07255C
Zuo GH, Kang SG, Xiu P, Zhao YL, Zhou RH (2013) Interactions between proteins and carbon-based nanoparticles: exploring the origin of nanotoxicity at the molecular level. Small 9(9–10):1546–1556. doi:10.1002/smll.201201381
Acknowledgments
This work is partially supported by the National Basic Research Program of China (973 Program Grant No. 2014CB931900), National Natural Science Foundation of China (21207164), A Project Funded by the Priority Academic Program Development of Jiangsu Higher Education Institutions (PAPD), and Jiangsu Provincial Key Laboratory of Radiation Medicine and Protection.
Author information
Authors and Affiliations
Corresponding author
Additional information
Cuicui Ge and Jian Tian have contributed equally to this work.
Rights and permissions
About this article
Cite this article
Ge, C., Tian, J., Zhao, Y. et al. Towards understanding of nanoparticle–protein corona. Arch Toxicol 89, 519–539 (2015). https://doi.org/10.1007/s00204-015-1458-0
Received:
Accepted:
Published:
Issue Date:
DOI: https://doi.org/10.1007/s00204-015-1458-0