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Merging Worlds of Nanomaterials and Biological Environment: Factors Governing Protein Corona Formation on Nanoparticles and Its Biological Consequences

Foroozandeh, Parisa, Aziz, Azlan Abdul·2015·Nanoscale Research Letters
DOI 10.1186/s11671-015-0922-3PMC PMC4437989
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Fig. 1 Schematic representation of exchange/interaction scenarios and of the structure of protein-nanoparticle. a Schematic representation of the possible exchange/interaction scenarios at the bionanointerface at the cellular level. b Schematic drawing of the structure of protein-nanoparticle in blood plasma confirming the existence of various protein binding (e.g., an outer weakly interacting layer of protein (full red arrows) and a hard slowly exchanging corona of proteins (right) (adapted with permission from [35]))
Fig. 1 Schematic representation of exchange/interaction scenarios and of the structure of protein-nanoparticle. a Schematic representation of the possible exchange/interaction scenarios at the bionanointerface at the cellular level. b Schematic drawing of the structure of protein-nanoparticle in blood plasma confirming the existence of various protein binding (e.g., an outer weakly interacting layer of protein (full red arrows) and a hard slowly exchanging corona of proteins (right) (adapted with permission from [35]))CC BY · PubMed Central
Fig. 2 Schematic illustration of difference in the hard corona composition on nanoparticles depending on the route of administration; intravenous and inhalation. The proteins that adsorbs on nanoparticle may vary depending on its exposure to the different types of biological fluids in the human body
Fig. 2 Schematic illustration of difference in the hard corona composition on nanoparticles depending on the route of administration; intravenous and inhalation. The proteins that adsorbs on nanoparticle may vary depending on its exposure to the different types of biological fluids in the human bodyCC BY · PubMed Central
Fig. 3 Graphical representation of plasma concentration effect on the thickness of hard corona formation on nanoparticles. The thickness of hard protein corona increases reciprocally as the concentration of plasma increases
Fig. 3 Graphical representation of plasma concentration effect on the thickness of hard corona formation on nanoparticles. The thickness of hard protein corona increases reciprocally as the concentration of plasma increasesCC BY · PubMed Central
Fig. 4 Scheme showing positively charged nanoparticles having a greater efficiency in cell membrane penetration and cellular internalization than negatively charged nanoparticles
Fig. 4 Scheme showing positively charged nanoparticles having a greater efficiency in cell membrane penetration and cellular internalization than negatively charged nanoparticlesCC BY · PubMed Central

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Research works printed but not linked: 73

  1. Albanese A, Tang PS, Chan WC. The effect of nanoparticle size, shape, and surface chemistry on biological systems. Annu Rev Biomed Eng. 2012;14:1–16. · DOI · Paper page
  2. Rauch J, Kolch W, Laurent S, Mahmoudi M. Big signals from small particles: regulation of cell signaling pathways by nanoparticles. Chem Rev. 2013;113(5):3391–406. · DOI
  3. Steigerwald ML, Brus LE. Semiconductor crystallites: a class of large molecules. Acc Chem Res. 1990;23(6):183–8. · DOI
  4. Wang Y. Nonlinear optical properties of nanometer-sized semiconductor clusters. Acc Chem Res. 1991;24(5):133–9. · DOI
  5. Weller H. Quantized semiconductor particles: a novel state of matter for materials science. Adv Mater. 1993;5(2):88–95. · DOI
  6. Mahmoudi M, Sant S, Wang B, Laurent S, Sen T. Superparamagnetic iron oxide nanoparticles (SPIONs): development, surface modification and applications in chemotherapy. Adv Drug Deliv Rev. 2011;63(1–2):24–46. · DOI
  7. Ragnaill MN, Brown M, Ye D, Bramini M, Callanan S, Lynch I, et al. Internal benchmarking of a human blood–brain barrier cell model for screening of nanoparticle uptake and transcytosis. Eur J Pharm Biopharm. 2011;77(3):360–7. · DOI
  8. Cho K, Wang X, Nie S, Chen Z, Shin DM. Therapeutic nanoparticles for drug delivery in cancer. Clin Cancer Res. 2008;14(5):1310–6. · DOI
  9. Ditto AJ, Shah PN, Yun YH. Non-viral gene delivery using nanoparticles. Expert Opin Drug Deliv. 2009;6(11):1149–60. · DOI
  10. Rosi NL, Giljohann DA, Thaxton CS, Lytton-Jean AK, Han MS, Mirkin CA. Oligonucleotide-modified gold nanoparticles for intracellular gene regulation. Science. 2006;312(5776):1027–30. · DOI
  11. Tanaka T, Mangala LS, Vivas-Mejia PE, Nieves-Alicea R, Mann AP, Mora E, et al. Sustained small interfering RNA delivery by mesoporous silicon particles. Cancer Res. 2010;70(9):3687–96. · DOI
  12. Xu C, Mu L, Roes I, Miranda-Nieves D, Nahrendorf M, Ankrum JA, et al. Nanoparticle-based monitoring of cell therapy. Nanotechnology. 2011;22(49):494001. · DOI
  13. Liang XJ, Meng H, Wang YZ, He HY, Meng J, Lu J, et al. Metallofullerene nanoparticles circumvent tumor resistance to cisplatin by reactivating endocytosis. Proc Natl Acad Sci. 2010;107(16):7449–54. · DOI
  14. Yan L, Zhao F, Li S, Hu Z, Zhao Y. Low-toxic and safe nanomaterials by surface-chemical design, carbon nanotubes, fullerenes, metallofullerenes, and graphenes. Nanoscale. 2011;3(2):362–82. · DOI
  15. Lee JH, Jang JT, Choi JS, Moon SH, Noh SH, Kim JW, et al. Exchange-coupled magnetic nanoparticles for efficient heat induction. Nat Nanotechnol. 2011;6(7):418–22. · DOI
  16. Kircher MF, de la Zerda A, Jokerst JV, Zavaleta CL, Kempen PJ, Mittra E, et al. A brain tumor molecular imaging strategy using a new triple-modality MRI-photoacoustic-Raman nanoparticle. Nat Med. 2012;18(5):829–34. · DOI
  17. Rogers WJ, Meyer CH, Kramer CM. Technology insight: in vivo cell tracking by use of MRI. Nat Clin Pract Cardiovasc Med. 2006;3(10):554–62. · DOI
  18. Eigenheer R, Castellanos ER, Nakamoto MY, Gerner KT, Lampe AM, Wheeler KE. Silver nanoparticle protein corona composition compared across engineered particle properties and environmentally relevant reaction conditions. Environ Sci: Nano. 2014;1(3):238.
  19. Mahmoudi M, Lynch I, Ejtehadi MR, Monopoli MP, Bombelli FB, Laurent S. Protein—nanoparticle interactions: opportunities and challenges. Chem Rev. 2011;111(9):5610–37. · DOI
  20. Monopoli MP, Åberg C, Salvati A, Dawson KA. Biomolecular coronas provide the biological identity of nanosized materials. Nat Nanotechnol. 2012;7(12):779–86. · DOI · Paper page
  21. Ghavami M, Saffar S, Abd Emamy B, Peirovi A, Shokrgozar MA, Serpooshan V, et al. Plasma concentration gradient influences the protein corona decoration on nanoparticles. RSC Adv. 2013;3(4):1119–26. · DOI
  22. Nel AE, Mädler L, Velegol D, Xia T, Hoek EM, Somasundaran P, et al. Understanding biophysicochemical interactions at the nano-bio interface. Nat Mater. 2009;8(7):543–57. · DOI · Paper page
  23. Treuel L, Nienhaus GU. Toward a molecular understanding of nanoparticle-protein interactions. Biophys Rev. 2012;4(2):137–47. · DOI
  24. Rahman M, Laurent S, Tawil N, Yahia LH, Mahmoudi M. Nanoparticle and protein corona. In: Protein-nanoparticle interactions. New York: Springer; 2013. p. 21–44. · DOI
  25. Walkey CD, Olsen JB, Song F, Liu R, Guo H, Olsen DWH, et al. Protein corona fingerprinting predicts the cellular interaction of gold and silver nanoparticles. ACS Nano. 2014;8(3):2439–55. · DOI
  26. Lesniak A, Fenaroli F, Monopoli MP, Åberg C, Dawson KA, Salvati A. Effects of the presence or absence of a protein corona on silica nanoparticle uptake and impact on cells. ACS Nano. 2012;6(7):5845–57. · DOI · Paper page
  27. Laurent S, Burtea C, Thirifays C, Rezaee F, Mahmoudi M. Significance of cell “observer” and protein source in nanobiosciences. J Colloid Interface Sci. 2013;392:431–45. · DOI
  28. Cedervall T, Lynch I, Lindman S, Berggard T, Thulin E, Nilsson H, et al. Understanding the nanoparticle-protein corona using methods to quantify exchange rates and affinities of proteins for nanoparticles. Proc Natl Acad Sci. 2007;104(7):2050–5. · DOI · Paper page
  29. Lacerda SHDP, Park JJ, Meuse C, Pristinski D, Becker ML, Karim A, et al. Interaction of gold nanoparticles with common human blood proteins. ACS Nano. 2009;4(1):365–79. · DOI
  30. Lundqvist M, Stigler J, Elia G, Lynch I, Cedervall T, Dawson KA. Nanoparticle size and surface properties determine the protein corona with possible implications for biological impacts. Proc Natl Acad Sci. 2008;105(38):14265–70. · DOI · Paper page
  31. Walczyk D, Bombelli FB, Monopoli MP, Lynch I, Dawson KA. What the cell “sees” in bionanoscience. J Am Chem Soc. 2010;132(16):5761–8. · DOI
  32. Cedervall T, Lynch I, Foy M, Berggård T, Donnelly SC, Cagney G, et al. Detailed identification of plasma proteins adsorbed on copolymer nanoparticles. Angew Chem Int Ed. 2007;46(30):5754–6. · DOI
  33. Mahmoudi M, Sahraian MA, Shokrgozar MA, Laurent S. Superparamagnetic iron oxide nanoparticles: promises for diagnosis and treatment of multiple sclerosis. ACS Chem Neurosci. 2011;2(3):118–40. · DOI
  34. Saptarshi SR, Duschl A, Lopata AL. Interaction of nanoparticles with proteins: relation to bio-reactivity of the nanoparticle. J Nanobiotechnol. 2013;11:26. · DOI
  35. Lundqvist M, Stigler J, Cedervall T, Berggård T, Flanagan MB, Lynch I, et al. The evolution of the protein corona around nanoparticles: a test study. ACS Nano. 2011;5(9):7503–9. · DOI · Paper page
  36. Simberg D, Park JH, Karmali PP, Zhang WM, Merkulov S, McCrae K, et al. Differential proteomics analysis of the surface heterogeneity of dextran iron oxide nanoparticles and the implications for their in vivo clearance. Biomaterials. 2009;30(23):3926–33. · DOI
  37. Aggarwal P, Hall JB, McLeland CB, Dobrovolskaia MA, McNeil SE. Nanoparticle interaction with plasma proteins as it relates to particle biodistribution, biocompatibility and therapeutic efficacy. Adv Drug Deliv Rev. 2009;61(6):428–37. · DOI · Paper page
  38. Ehrenberg MS, Friedman AE, Finkelstein JN, Oberdorster G, McGrath JL. The influence of protein adsorption on nanoparticle association with cultured endothelial cells. Biomaterials. 2009;30(4):603–10. · DOI · Paper page
  39. Harnisch S, Müller RH. Adsorption kinetics of plasma proteins on oil-in-water emulsions for parenteral nutrition. Eur J Pharm Biopharm. 2000;49(1):41–6. · DOI
  40. Göppert TM, Müller RH. Polysorbate-stabilized solid lipid nanoparticles as colloidal carriers for intravenous targeting of drugs to the brain: comparison of plasma protein adsorption patterns. J Drug Target. 2005;13(3):179–87. · DOI
  41. Vroman L, Adams A, Fischer G, Munoz P. Interaction of high molecular weight kininogen, factor XII, and fibrinogen. Blood. 1980;55(1):156–9. · DOI · Paper page
  42. Göppert TM, Müller RH. Adsorption kinetics of plasma proteins on solid lipid nanoparticles for drug targeting. Int J Pharm. 2005;302(1–2):172–86. · DOI
  43. Jansch M, Stumpf P, Graf C, Rühl E, Müller RH. Adsorption kinetics of plasma proteins on ultrasmall superparamagnetic iron oxide (USPIO) nanoparticles. Int J Pharm. 2012;428(1–2):125–33. · DOI
  44. Gessner A, Waicz R, Lieske A, Paulke B, Mader K, Muller RH. Nanoparticles with decreasing surface hydrophobicities: influence on plasma protein adsorption. Int J Pharm. 2000;196(2):245–9. · DOI
  45. Treuel L. How protein adsorption shapes the biological identity of NPs—where do we stand? J Phys Chem Biophys. 2013;3:e113. · DOI
  46. Buijs J, Vera CC, Ayala E, Steensma E, Håkansson P, Oscarsson S. Conformational stability of adsorbed insulin studied with mass spectrometry and hydrogen exchange. Anal Chem. 1999;71(15):3219–25. · DOI
  47. Mahmoudi M, Sardari S, Shokrgozar MA, Laurent S, Stroeve P. Irreversible changes in protein conformation due to interaction with superparamagnetic iron oxide nanoparticles. Nanoscale. 2011;3(3):1127–38.
  48. Shang L, Wang Y, Jiang J, Dong S. pH-dependent protein conformational changes in albumin: gold nanoparticle bioconjugates: a spectroscopic study. Langmuir. 2007;23(5):2714–21. · DOI
  49. Nagayama S, Ogawara K-i, Fukuoka Y, Higaki K, Kimura T. Time-dependent changes in opsonin amount associated on nanoparticles alter their hepatic uptake characteristics. Int J Pharm. 2007;342(1–2):215–21. · DOI
  50. Deng ZJ, Mortimer G, Schiller T, Musumeci A, Martin D, Minchin RF. Differential plasma protein binding to metal oxide nanoparticles. Nanotechnology. 2009;20(45):455101. · DOI
  51. Lynch I, Dawson KA. Protein-nanoparticle interactions. Nano Today. 2008;3(1–2):40–7. · DOI
  52. Hill HD, Millstone JE, Banholzer MJ, Mirkin CA. The role radius of curvature plays in thiolated oligonucleotide loading on gold nanoparticles. ACS Nano. 2009;3(2):418–24. · DOI
  53. Tenzer S, Docter D, Rosfa S, Wlodarski A, Kuharev J, Rekik A, et al. Nanoparticle size is a critical physicochemical determinant of the human blood plasma corona: a comprehensive quantitative proteomic analysis. ACS Nano. 2011;5:7155–67. · DOI
  54. Dobrovolskaia MA, Patri AK, Zheng J, Clogston JD, Ayub N, Aggarwal P, et al. Interaction of colloidal gold nanoparticles with human blood: effects on particle size and analysis of plasma protein binding profiles. Nanomed Nanotechnol Biol Med. 2009;5(2):106–17. · DOI
  55. Vertegel AA, Siegel RW, Dordick JS. Silica nanoparticle size influences the structure and enzymatic activity of adsorbed lysozyme. Langmuir. 2004;20(16):6800–7. · DOI
  56. Cox MC, Barnham KJ, Frenkiel TA, Hoeschele JD, Mason AB, He Q-Y, et al. Identification of platination sites on human serum transferrin using 13C and 15N NMR spectroscopy. JBIC J Biol Inorg Chem. 1999;4(5):621–31. · DOI
  57. Gref R, Lück M, Quellec P, Marchand M, Dellacherie E, Harnisch S, et al. ‘Stealth’ corona-core nanoparticles surface modified by polyethylene glycol (PEG): influences of the corona (PEG chain length and surface density) and of the core composition on phagocytic uptake and plasma protein adsorption. Colloids Surf B: Biointerfaces. 2000;18(3–4):301–13. · DOI
  58. Perry JL, Reuter KG, Kai MP, Herlihy KP, Jones SW, Luft JC, et al. PEGylated PRINT nanoparticles: the impact of PEG density on protein binding, macrophage association, biodistribution, and pharmacokinetics. Nano Lett. 2012;12(10):5304–10. · DOI
  59. Moghimi SM, Muir I, Illum L, Davis SS, Kolb-Bachofen V. Coating particles with a block co-polymer (poloxamine-908) suppresses opsonization but permits the activity of dysopsonins in the serum. Biochimica et Biophysica Acta (BBA)-Molecular. Cell Res. 1993;1179(2):157–65.
  60. Dutta D, Sundaram SK, Teeguarden JG, Riley BJ, Fifield LS, Jacobs JM, et al. Adsorbed proteins influence the biological activity and molecular targeting of nanomaterials. Toxicol Sci. 2007;100(1):303–15. · DOI
  61. Gessner A, Lieske A, Paulke BR, Müller RH. Influence of surface charge density on protein adsorption on polymeric nanoparticles: analysis by two-dimensional electrophoresis. Eur J Pharm Biopharm. 2002;54(2):165–70. · DOI
  62. Roach P, Farrar D, Perry CC. Interpretation of protein adsorption: surface-induced conformational changes. J Am Chem Soc. 2005;127(22):8168–73. · DOI
  63. Maiorano G, Sabella S, Sorce B, Brunetti V, Malvindi MA, Cingolani R, et al. Effects of cell culture media on the dynamic formation of protein − nanoparticle complexes and influence on the cellular response. ACS Nano. 2010;4(12):7481–91. · DOI · Paper page
  64. Albanese A, Walkey CD, Olsen JB, Guo H, Emili A, Chan WCW. Secreted biomolecules alter the biological identity and cellular interactions of nanoparticles. ACS Nano. 2014;8(6):5515–26. · DOI · Paper page
  65. Laurent S, Burtea C, Thirifays C, Hafeli UO, Mahmoudi M. Crucial ignored parameters on nanotoxicology: the importance of toxicity assay modifications and “cell vision”. PLoS ONE. 2012;7(1):e29997. · DOI · Paper page
  66. Rhoades R, Pflanzer RG. Human physiology. 4th ed. Fort Worth: Saunders College Publication; 1989.
  67. Petersdorf R. Chap 12. Chills and fever. In: Wintrob MM, Thorn GW, Adams RD, Braaunwald E, Isselbacher KJ, Petersdorf RG, editors. Harrison’s principles of internal medicine. 7th ed. New York: McGraw-Hill; 1974. p. 58–60.
  68. Yang J-M, Yang H, Lin L. Quantum dot nano thermometers reveal heterogeneous local thermogenesis in living cells. ACS Nano. 2011;5(6):5067–71. · DOI
  69. Hasday JD, Singh IS. Fever and the heat shock response: distinct, partially overlapping processes. Cell Stress Chaperones. 2000;5(5):471–80. · DOI
  70. Mahmoudi M, Abdelmonem AM, Behzadi S, Clement JH, Dutz S, Ejtehadi MR, et al. Temperature: the “ignored” factor at the nanobio interface. ACS Nano. 2013;7(8):6555–62. · DOI
  71. Mahmoudi M, Lohse SE, Murphy CJ, Fathizadeh A, Montazeri A, Suslick KS. Variation of protein corona composition of gold nanoparticles following plasmonic heating. Nano Lett. 2014;14(1):6–12. · DOI
  72. Mahmoudi M, Meng J, Xue X, Liang XJ, Rahman M, Pfeiffer C, et al. Interaction of stable colloidal nanoparticles with cellular membranes. Biotechnol Adv. 2014;32(4):679–92. · DOI
  73. Lesniak A, Salvati A, Santos-Martinez MJ, Radomski MW, Dawson KA, Åberg C. Nanoparticle adhesion to the cell membrane and its effect on nanoparticle uptake efficiency. J Am Chem Soc. 2013;135(4):1438–44. · DOI

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Metadata

Authors
Foroozandeh, P., & Aziz, A. A.
Venue
Nanoscale Research Letters
Publisher
Springer Science and Business Media LLC
Published
2015-05-16
Volume
10
Issue
1
ISSN
  • 1931-7573
  • 1556-276X
DOI
10.1186/s11671-015-0922-3
PMC
PMC4437989
Cited by
143
References
4
Language
en
Licence
creativecommons.org/licenses/by/4.0 (unspecified)

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Foroozandeh, P., & Aziz, A. A. (2015). Merging Worlds of Nanomaterials and Biological Environment: Factors Governing Protein Corona Formation on Nanoparticles and Its Biological Consequences. Nanoscale Research Letters. https://doi.org/10.1186/s11671-015-0922-3