countering biomolecular corona formation and uptake by the mononuclear phagocyte system.
Small 10(13), 2516–2529 (2014)
10. P. Zhang, F. Sun, C. Tsao, S. Liu, P. Jain, A. Sinclair et al., Zwitterionic gel encapsulation
promotes protein stability, enhances pharmacokinetics, and reduces immunogenicity. Proc.
Natl. Acad. Sci. U S A 112(39), 12046–12051 (2015)
11. P.L. Turecek, M.J. Bossard, F. Schoetens, I.A. Ivens, PEGylation of biopharmaceuticals: a
review of chemistry and nonclinical safety information of approved drugs. J. Pharm. Sci. 105
(2), 460–475 (2016)
12. M.J. Roberts, M.D. Bentley, J.M. Harris, Chemistry for peptide and protein PEGylation. Adv.
Drug Deliv. Rev. 54(4), 459–476 (2002)
13. L. Wu, J. Chen, Y. Wu, B. Zhang, X. Cai, Z. Zhang et al., Precise and combinatorial
PEGylation generates a low-immunogenic and stable form of human growth hormone.
J. Control Release 249, 84–93 (2017)
14. 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)
15. 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)
16. 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)
17. Y. Yan, K.T. Gause, M.M. Kamphuis, C.S. Ang, N.M. O’Brien-Simpson, J.C. Lenzo 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(12), 10960–10970 (2013)
18. 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)
19. D. Docter, D. Westmeier, M. Markiewicz, S. Stolte, S.K. Knauer, R.H. Stauber, The
nanoparticle biomolecule corona: lessons learned—challenge accepted? Chem. Soc. Rev. 44
(17), 6094–6121 (2015)
20. S. Tenzer, D. Docter, J. Kuharev, A. Musyanovych, V. Fetz, R. Hecht et al., Rapid formation
of plasma protein corona critically affects nanoparticle pathophysiology. Nat. Nanotechnol. 8
(10), 772–781 (2013)
21. C.D. Walkey, J.B. Olsen, F. Song, R. Liu, H. Guo, D.W. Olsen et al., Protein corona
fingerprinting predicts the cellular interaction of gold and silver nanoparticles. ACS Nano 8
(3), 2439–2455 (2014)
22. C. Corbo, R. Molinaro, A. Parodi, N.E. Toledano Furman, F. Salvatore et al., The impact of
nanoparticle protein corona on cytotoxicity, immunotoxicity and target drug delivery.
Nanomed. (Lond). 11(1), 81–100 (2016)
23. M. Hadjidemetriou, Z. Al-Ahmady, M. Mazza, R.F. Collins, K. Dawson, K. Kostarelos, In
vivo biomolecule corona around blood-circulating, clinically used and antibody-targeted lipid
bilayer nanoscale vesicles. ACS Nano 9(8), 8142–8156 (2015)
24. S. Huo, S. Chen, N. Gong, J. Liu, X. Li, Y. Zhao et al., Ultrasmall gold nanoparticles behavior
in vivo modulated by surface polyethylene glycol (PEG) grafting. Bioconjug. Chem. 28(1),
239–243 (2017)
25. B. Kang, P. Okwieka, S. Schöttler, S. Winzen, J. Langhanki, K. Mohr et al.,
Carbohydrate-based nanocarriers exhibiting specific cell targeting with minimum influence
from the protein corona. Angew. Chem. Int. Ed. Engl. 54(25), 7436–7440 (2015)
26. Z. Amoozgar, Y. Yeo, Recent advances in stealth coating of nanoparticle drug delivery
systems. Wiley Interdiscip. Rev. Nanomed. Nanobiotechnol. 4(2), 219–233 (2012)
27. 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)
18 Polyethylene Glycolation (PEGylation) and the Similar
343
Small 10(13), 2516–2529 (2014)
10. P. Zhang, F. Sun, C. Tsao, S. Liu, P. Jain, A. Sinclair et al., Zwitterionic gel encapsulation
promotes protein stability, enhances pharmacokinetics, and reduces immunogenicity. Proc.
Natl. Acad. Sci. U S A 112(39), 12046–12051 (2015)
11. P.L. Turecek, M.J. Bossard, F. Schoetens, I.A. Ivens, PEGylation of biopharmaceuticals: a
review of chemistry and nonclinical safety information of approved drugs. J. Pharm. Sci. 105
(2), 460–475 (2016)
12. M.J. Roberts, M.D. Bentley, J.M. Harris, Chemistry for peptide and protein PEGylation. Adv.
Drug Deliv. Rev. 54(4), 459–476 (2002)
13. L. Wu, J. Chen, Y. Wu, B. Zhang, X. Cai, Z. Zhang et al., Precise and combinatorial
PEGylation generates a low-immunogenic and stable form of human growth hormone.
J. Control Release 249, 84–93 (2017)
14. 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)
15. 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)
16. 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)
17. Y. Yan, K.T. Gause, M.M. Kamphuis, C.S. Ang, N.M. O’Brien-Simpson, J.C. Lenzo 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(12), 10960–10970 (2013)
18. 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)
19. D. Docter, D. Westmeier, M. Markiewicz, S. Stolte, S.K. Knauer, R.H. Stauber, The
nanoparticle biomolecule corona: lessons learned—challenge accepted? Chem. Soc. Rev. 44
(17), 6094–6121 (2015)
20. S. Tenzer, D. Docter, J. Kuharev, A. Musyanovych, V. Fetz, R. Hecht et al., Rapid formation
of plasma protein corona critically affects nanoparticle pathophysiology. Nat. Nanotechnol. 8
(10), 772–781 (2013)
21. C.D. Walkey, J.B. Olsen, F. Song, R. Liu, H. Guo, D.W. Olsen et al., Protein corona
fingerprinting predicts the cellular interaction of gold and silver nanoparticles. ACS Nano 8
(3), 2439–2455 (2014)
22. C. Corbo, R. Molinaro, A. Parodi, N.E. Toledano Furman, F. Salvatore et al., The impact of
nanoparticle protein corona on cytotoxicity, immunotoxicity and target drug delivery.
Nanomed. (Lond). 11(1), 81–100 (2016)
23. M. Hadjidemetriou, Z. Al-Ahmady, M. Mazza, R.F. Collins, K. Dawson, K. Kostarelos, In
vivo biomolecule corona around blood-circulating, clinically used and antibody-targeted lipid
bilayer nanoscale vesicles. ACS Nano 9(8), 8142–8156 (2015)
24. S. Huo, S. Chen, N. Gong, J. Liu, X. Li, Y. Zhao et al., Ultrasmall gold nanoparticles behavior
in vivo modulated by surface polyethylene glycol (PEG) grafting. Bioconjug. Chem. 28(1),
239–243 (2017)
25. B. Kang, P. Okwieka, S. Schöttler, S. Winzen, J. Langhanki, K. Mohr et al.,
Carbohydrate-based nanocarriers exhibiting specific cell targeting with minimum influence
from the protein corona. Angew. Chem. Int. Ed. Engl. 54(25), 7436–7440 (2015)
26. Z. Amoozgar, Y. Yeo, Recent advances in stealth coating of nanoparticle drug delivery
systems. Wiley Interdiscip. Rev. Nanomed. Nanobiotechnol. 4(2), 219–233 (2012)
27. 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)
18 Polyethylene Glycolation (PEGylation) and the Similar
343