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37. M. Lundqvist, J. Stigler, G. Elia, I. Lynch, T. Cedervall, K.A. Dawson, Nanoparticle size and
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39. S. Milani, F.B. Bombelli, A.S. Pitek, K.A. Dawson, J. Rädler, Reversible versus irreversible
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42. A. Salvati, A.S. Pitek, M.P. Monopoli, K. Prapainop, F.B. Bombelli, D.R. Hristov et al.,
Transferrin-functionalized nanoparticles lose their targeting capabilities when a biomolecule
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43. M.P. Monopoli, C. Aberg, A. Salvati, K.A. Dawson, Biomolecular coronas provide the
biological identity of nanosized materials. Nat. Nanotechnol. 7(12), 779–786 (2012)
44. S. Schöttler, K. Landfester, V. Mailänder, Controlling the stealth effect of nanocarriers
through understanding the protein corona. Angew. Chem. Int. Ed. Engl. 55(31), 8806–8815
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45. M. Cataldi, C. Vigliotti, T. Mosca, M. Cammarota, D. Capone, Emerging role of the spleen in
the pharmacokinetics of monoclonal antibodies, nanoparticles and exosomes. Int. J. Mol. Sci.
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46. W. Wang, E.Q. Wang, J.P. Balthasar, Monoclonal antibody pharmacokinetics and
pharmacodynamics. Clin. Pharmacol. Ther. 84(5), 548–558 (2008)
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Immunol. 7(9), 715–725 (2007)
48. J.L. Perry, K.G. Reuter, M.P. Kai, K.P. Herlihy, S.W. Jones, J.C. Luft et al.,
PEGylated PRINT nanoparticles: the impact of PEG density on protein binding, macrophage
association, biodistribution, and pharmacokinetics. Nano Lett. 12(10), 5304–5310 (2012)
49. A.S. Abu Lila, H. Kiwada, T. Ishida, The accelerated blood clearance (ABC) phenomenon:
clinical challenge and approaches to manage. J. Control Release 172(1), 38–47 (2013)
50. T. Shimizu, T. Ishida, H. Kiwada, Transport of PEGylated liposomes from the splenic
marginal zone to the follicle in the induction phase of the accelerated blood clearance
phenomenon. Immunobiology 218(5), 725–732 (2013)
51. S. Shi, Biologics: an update and challenge of their pharmacokinetics. Curr. Drug Metab. 15
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52. J.W. Lee, ADME of monoclonal antibody biotherapeutics: knowledge gaps and emerging
tools. Bioanalysis 5(16), 2003–2014 (2013)
53. P. Chames, M. Van Regenmortel, E. Weiss, D. Baty, Therapeutic antibodies: successes,
limitations and hopes for the future. Br. J. Pharmacol. 157(2), 220–233 (2009)
406
D. S. Lee and Y. K. Shin
systems. Wiley Interdiscip. Rev. Nanomed. Nanobiotechnol. 4(2), 219–233 (2012)
35. S. Mondini, M. Leonzino, C. Drago, A.M. Ferretti, S. Usseglio, D. Maggioni et al.,
Zwitterion-coated iron oxide nanoparticles: surface chemistry and intracellular uptake by
hepatocarcinoma (HepG2) cells. Langmuir 31(26), 7381–7390 (2015)
36. T. Cedervall, I. Lynch, S. Lindman, T. Berggård, E. Thulin, H. Nilsson 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(7), 2050–2055 (2007)
37. M. Lundqvist, J. Stigler, G. Elia, I. Lynch, T. Cedervall, K.A. Dawson, Nanoparticle size and
surface properties determine the protein corona with possible implications for biological
impacts. Proc. Natl. Acad. Sci. USA 105(38), 14265–14270 (2008)
38. P. Aggarwal, J.B. Hall, C.B. McLeland, M.A. Dobrovolskaia, S.E. McNeil, Nanoparticle
interaction with plasma proteins as it relates to particle biodistribution, biocompatibility and
therapeutic efficacy. Adv. Drug Deliv. Rev. 61(6), 428–437 (2009)
39. S. Milani, F.B. Bombelli, A.S. Pitek, K.A. Dawson, J. Rädler, Reversible versus irreversible
binding of transferrin to polystyrene nanoparticles: soft and hard corona. ACS Nano. 6(3),
2532–2541 (2012)
40. P.M. Kelly, C. Åberg, E. Polo, A. O’Connell, J. Cookman, J. Fallon et al., Mapping protein
binding sites on the biomolecular corona of nanoparticles. Nat. Nanotechnol. 10(5), 472–479
(2015)
41. A. Lesniak, F. Fenaroli, M.P. Monopoli, C. Åberg, K.A. Dawson, A. Salvati, Effects of the
presence or absence of a protein corona on silica nanoparticle uptake and impact on cells.
ACS Nano. 6(7), 5845–5857 (2012)
42. A. Salvati, A.S. Pitek, M.P. Monopoli, K. Prapainop, F.B. Bombelli, D.R. Hristov et al.,
Transferrin-functionalized nanoparticles lose their targeting capabilities when a biomolecule
corona adsorbs on the surface. Nat. Nanotechnol. 8(2), 137–143 (2013)
43. M.P. Monopoli, C. Aberg, A. Salvati, K.A. Dawson, Biomolecular coronas provide the
biological identity of nanosized materials. Nat. Nanotechnol. 7(12), 779–786 (2012)
44. S. Schöttler, K. Landfester, V. Mailänder, Controlling the stealth effect of nanocarriers
through understanding the protein corona. Angew. Chem. Int. Ed. Engl. 55(31), 8806–8815
(2016)
45. M. Cataldi, C. Vigliotti, T. Mosca, M. Cammarota, D. Capone, Emerging role of the spleen in
the pharmacokinetics of monoclonal antibodies, nanoparticles and exosomes. Int. J. Mol. Sci.
18(6), E1249 (2017)
46. W. Wang, E.Q. Wang, J.P. Balthasar, Monoclonal antibody pharmacokinetics and
pharmacodynamics. Clin. Pharmacol. Ther. 84(5), 548–558 (2008)
47. D.C. Roopenian, S. Akilesh, FcRn: the neonatal Fc receptor comes of age. Nat. Rev.
Immunol. 7(9), 715–725 (2007)
48. J.L. Perry, K.G. Reuter, M.P. Kai, K.P. Herlihy, S.W. Jones, J.C. Luft et al.,
PEGylated PRINT nanoparticles: the impact of PEG density on protein binding, macrophage
association, biodistribution, and pharmacokinetics. Nano Lett. 12(10), 5304–5310 (2012)
49. A.S. Abu Lila, H. Kiwada, T. Ishida, The accelerated blood clearance (ABC) phenomenon:
clinical challenge and approaches to manage. J. Control Release 172(1), 38–47 (2013)
50. T. Shimizu, T. Ishida, H. Kiwada, Transport of PEGylated liposomes from the splenic
marginal zone to the follicle in the induction phase of the accelerated blood clearance
phenomenon. Immunobiology 218(5), 725–732 (2013)
51. S. Shi, Biologics: an update and challenge of their pharmacokinetics. Curr. Drug Metab. 15
(3), 271–290 (2014)
52. J.W. Lee, ADME of monoclonal antibody biotherapeutics: knowledge gaps and emerging
tools. Bioanalysis 5(16), 2003–2014 (2013)
53. P. Chames, M. Van Regenmortel, E. Weiss, D. Baty, Therapeutic antibodies: successes,
limitations and hopes for the future. Br. J. Pharmacol. 157(2), 220–233 (2009)
406
D. S. Lee and Y. K. Shin
