Effects of Surface Coating on Nanoparticle-Protein Adsorption Selectivity

Article

Abstract

Negatively charged, uni-sized naked gold (Au) and coated poly (acrylic acid) (PAA)—polyethyleneimine (PEI)-Au (PPAu) nanoparticles (NP)s were incubated with four proteins of different molecular weights: bovine serum albumin (BSA) ~ 67 kDa, cationic trypsin ~ 23.3 kDa, LL-37 peptide ~ 4.5 kDa, and PK(FK)5PK peptide ~ 1.9 kDa. Different interaction kinetics were observed and analyzed by cryogenic transmission electron microscopy (cryoTEM) and UV-Vis spectroscopy. The naked Au NPs adsorbed all four proteins showing no selectivity towards any specific protein category, while PPAu NPs adsorbed only the LL-37 and PK(FK)5PK peptides (they did not adsorb BSA and cationic trypsin), thereby expressing selectivity to positively charged low molecular weight (LMW) proteins. Applying an interpretation of the Hill model, we showed that PPAu and naked Au NPs have similar affinity and cooperative binding behavior toward the PK(FK)5PK peptide. This study also supports the assumption that NP chemical composition may be a tunable property in NP design for specific applications such as LMW proteins’ harvesting, biosensing, and drug delivery systems. Although it may be speculated that surface structure may be shaped to enhance selective adsorption, this feature has not been demonstrated in the present study.

Lay Summary

Protein-NP interaction is an emerging field in biomedical research. Particularly Au NPs-protein interaction, due to the Au NPs promising medical applications inherited from their easy-to-make and surface functionalizing processes. This interaction depends on several factors, such as NP size, surface charge, and surface chemical composition and morphology. Herein, we studied the effect of NP surface coating on the adsorption behavior of various proteins of similar size, negatively charged naked Au, and coated PPAu NPs. Our findings suggest that the NPs’ surface morphology may play a major role in molecular weight (MW)-based NP-protein adsorption selectivity.

Future Work

Future work will focus on engineering new coated Au NPs with different polymers to gain better understanding regarding the effects of surface composition and manipulated morphology on the selective adsorption of proteins. Additionally, we will explore the potential role of selective protein adsorption in regenerative medicine bioresearch and applications.

Graphical Abstract

Keywords

Nanoparticles Morphology Protein corona Aggregation Nanoparticle-protein interaction 

References

  1. 1.
    Alivisatos P. The use of nanocrystals in biological detection. Nat Biotechnol. 2004;22(1):47–52.CrossRefGoogle Scholar
  2. 2.
    Casals E, Pfaller T, Duschl A, Oostingh GJ, Puntes V. Time evolution of the nanoparticle protein corona. ACS Nano. 2010;4(7):3623–32.CrossRefGoogle Scholar
  3. 3.
    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.CrossRefGoogle Scholar
  4. 4.
    Ge CC, et al. Binding of blood proteins to carbon nanotubes reduces cytotoxicity. Proc Natl Acad Sci U S A. 2011;108(41):16968–73.CrossRefGoogle Scholar
  5. 5.
    Lacerda SHD, et al. Interaction of gold nanoparticles with common human blood proteins. ACS Nano. 2010;4(1):365–79.CrossRefGoogle Scholar
  6. 6.
    Lynch I, Dawson KA. Protein-nanoparticle interactions. Nano Today. 2008;3(1–2):40–7.CrossRefGoogle Scholar
  7. 7.
    Mahato M, Pal P, Tah B, Ghosh M, Talapatra GB. Study of silver nanoparticle-hemoglobin interaction and composite formation. Colloids Surf B Biointerfaces. 2011;88(1):141–9.CrossRefGoogle Scholar
  8. 8.
    Monopoli MP, Walczyk D, Campbell A, Elia G, Lynch I, Baldelli Bombelli F, et al. Physical-chemical aspects of protein corona: relevance to in vitro and in vivo biological impacts of nanoparticles. J Am Chem Soc. 2011;133(8):2525–34.CrossRefGoogle Scholar
  9. 9.
    Ruh H, Kühl B, Brenner-Weiss G, Hopf C, Diabaté S, Weiss C. Identification of serum proteins bound to industrial nanomaterials. Toxicol Lett. 2012;208(1):41–50.CrossRefGoogle Scholar
  10. 10.
    Shemetov AA, Nabiev I, Sukhanova A. Molecular interaction of proteins and peptides with nanoparticles. ACS Nano. 2012;6(6):4585–602.CrossRefGoogle Scholar
  11. 11.
    Zhang DM, et al. Gold nanoparticles can induce the formation of protein-based aggregates at physiological pH. Nano Lett. 2009;9(2):666–71.CrossRefGoogle Scholar
  12. 12.
    Deng ZJ, Liang M, Monteiro M, Toth I, Minchin RF. Nanoparticle-induced unfolding of fibrinogen promotes Mac-1 receptor activation and inflammation. Nat Nanotechnol. 2011;6(1):39–44.CrossRefGoogle Scholar
  13. 13.
    Shrivastava S, Singh SK, Mukhopadhyay A, Sinha ASK, Mandal RK, Dash D. Negative regulation of fibrin polymerization and clot formation by nanoparticles of silver. Colloids Surf B Biointerfaces. 2011;82(1):241–6.CrossRefGoogle Scholar
  14. 14.
    Huang RX, et al. Effects of surface compositional and structural heterogeneity on nanoparticle-protein interactions: different protein configurations. ACS Nano. 2014;8(6):5402–12.CrossRefGoogle Scholar
  15. 15.
    Lynch I, et al. The nanoparticle-protein complex as a biological entity; a complex fluids and surface science challenge for the 21st century. Adv Colloid Interf Sci. 2007;134-35:167–74.CrossRefGoogle Scholar
  16. 16.
    Saha K, Rahimi M, Yazdani M, Kim ST, Moyano DF, Hou S, et al. Regulation of macrophage recognition through the interplay of nanoparticle surface functionality and protein corona. ACS Nano. 2016;10(4):4421–30.CrossRefGoogle Scholar
  17. 17.
    Charbgoo F, Nejabat M, Abnous K, Soltani F, Taghdisi SM, Alibolandi M, et al. Gold nanoparticle should understand protein corona for being a clinical nanomaterial. J Control Release. 2018;272:39–53.CrossRefGoogle Scholar
  18. 18.
    You CC, Miranda OR, Gider B, Ghosh PS, Kim IB, Erdogan B, et al. Detection and identification of proteins using nanoparticle-fluorescent polymer ‘chemical nose’ sensors. Nat Nanotechnol. 2007;2(5):318–23.CrossRefGoogle Scholar
  19. 19.
    Khoury LR, Goldbart R, Traitel T, Enden G, Kost J. Harvesting low molecular weight biomarkers using gold nanoparticles. ACS Nano. 2015;9(6):5750–9.CrossRefGoogle Scholar
  20. 20.
    Benetti F, Fedel M, Minati L, Speranza G, Migliaresi C. Gold nanoparticles: role of size and surface chemistry on blood protein adsorption. J Nanopart Res. 2013;15(6):1–9.CrossRefGoogle Scholar
  21. 21.
    Jiang X, Jiang J, Jin Y, Wang E, Dong S. Effect of colloidal gold size on the conformational changes of adsorbed cytochrome c: probing by circular dichroism, UV-visible, and infrared spectroscopy. Biomacromolecules. 2005;6(1):46–53.CrossRefGoogle Scholar
  22. 22.
    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 U S A. 2008;105(38):14265–70.CrossRefGoogle Scholar
  23. 23.
    Nel AE, Mädler L, Velegol D, Xia T, Hoek EMV, Somasundaran P, et al. Understanding biophysicochemical interactions at the nano-bio interface. Nat Mater. 2009;8(7):543–57.CrossRefGoogle Scholar
  24. 24.
    Chakraborty S, Joshi P, Shanker V, Ansari ZA, Singh SP, Chakrabarti P. Contrasting effect of gold nanoparticles and Nanorods with different surface modifications on the structure and activity of bovine serum albumin. Langmuir. 2011;27(12):7722–31.CrossRefGoogle Scholar
  25. 25.
    Chaudhary A, Gupta A, Khan S, Nandi CK. Morphological effect of gold nanoparticles on the adsorption of bovine serum albumin. Phys Chem Chem Phys. 2014;16(38):20471–82.CrossRefGoogle Scholar
  26. 26.
    Gagner JE, Lopez MD, Dordick JS, Siegel RW. Effect of gold nanoparticle morphology on adsorbed protein structure and function. Biomaterials. 2011;32(29):7241–52.CrossRefGoogle Scholar
  27. 27.
    Del Pino P, et al. Protein corona formation around nanoparticles—from the past to the future. Mater Horiz. 2014;1(3):301–13.CrossRefGoogle Scholar
  28. 28.
    Doyen M, Goole J, Bartik K, Bruylants G. Amino acid induced fractal aggregation of gold nanoparticles: why and how. J Colloid Interface Sci. 2016;464:160–6.CrossRefGoogle Scholar
  29. 29.
    Attia YA, et al. Photostability of gold nanoparticles with different shapes: the role of Ag clusters. Nano. 2015;7(26):11273–9.Google Scholar
  30. 30.
    Haiss W, Thanh NTK, Aveyard J, Fernig DG. Determination of size and concentration of gold nanoparticles from UV-Vis spectra. Anal Chem. 2007;79(11):4215–21.CrossRefGoogle Scholar
  31. 31.
    Storhoff JJ, Elghanian R, Mucic RC, Mirkin CA, Letsinger RL. One-pot colorimetric differentiation of polynucleotides with single base imperfections using gold nanoparticle probes. J Am Chem Soc. 1998;120(9):1959–64.CrossRefGoogle Scholar
  32. 32.
    Yu HH, Jiang DS. Spectroscopic studies on electrostatically self-assembled gold nanoparticulate thin films. Spectrosc Spectr Anal. 2002;22(3):511–4.Google Scholar
  33. 33.
    Jans H, Liu X, Austin L, Maes G, Huo Q. Dynamic light scattering as a powerful tool for gold nanoparticle bioconjugation and biomolecular binding studies. Anal Chem. 2009;81(22):9425–32.CrossRefGoogle Scholar
  34. 34.
    Shi XJ, Li D, Xie J, Wang S, Wu ZQ, Chen H. Spectroscopic investigation of the interactions between gold nanoparticles and bovine serum albumin. Chin Sci Bull. 2012;57(10):1109–15.CrossRefGoogle Scholar
  35. 35.
    Brewer SH, Glomm WR, Johnson MC, Knag MK, Franzen S. Probing BSA binding to citrate-coated gold nanoparticles and surfaces. Langmuir. 2005;21(20):9303–7.CrossRefGoogle Scholar
  36. 36.
    Gao DJ, et al. Studies on the interaction of colloidal gold and serum albumins by spectral methods. Spectrochim Acta A Mol Biomol Spectrosc. 2005;62(4–5):1203–8.CrossRefGoogle Scholar
  37. 37.
    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 U S A. 2007;104(7):2050–5.CrossRefGoogle Scholar
  38. 38.
    Dominguez-Medina S, Blankenburg J, Olson J, Landes CF, Link S. Adsorption of a protein monolayer via hydrophobic interactions prevents nanoparticle aggregation under harsh environmental conditions. ACS Sustain Chem Eng. 2013;1(7):833–42.CrossRefGoogle Scholar
  39. 39.
    Moerz ST, Kraegeloh A, Chanana M, Kraus T. Formation mechanism for stable hybrid clusters of proteins and nanoparticles. ACS Nano. 2015;9(7):6696–705.CrossRefGoogle Scholar
  40. 40.
    Erickson HP. Size and shape of protein molecules at the nanometer level determined by sedimentation, gel filtration, and electron microscopy. Biol Proced Online. 2009;11(1):32–51.CrossRefGoogle Scholar
  41. 41.
    Barrow CJ, Yasuda A, Kenny PTM, Zagorski MG. Solution conformations and aggregational properties of synthetic amyloid beta-peptides of Alzheimer’s disease: analysis of circular dichroism spectra. J Mol Biol. 1992;225(4):1075–93.CrossRefGoogle Scholar
  42. 42.
    Burdick D, Soreghan B, Kwon M, Kosmoski J, Knauer M, Henschen A, et al. Assembly and aggregation properties of synthetic Alzheimer’s A4/beta amyloid peptide analogs. J Biol Chem. 1992;267(1):546–54.Google Scholar
  43. 43.
    Kim HY, Choi I. Ultrafast colorimetric determination of predominant protein structure evolution with gold nanoplasmonic particles. Nano. 2016;8(4):1952–9.Google Scholar
  44. 44.
    Stine WB, et al. In vitro characterization of conditions for amyloid-beta peptide oligomerization and fibrillogenesis. J Biol Chem. 2003;278(13):11612–22.CrossRefGoogle Scholar
  45. 45.
    Walkey CD, Olsen JB, Guo H, Emili A, Chan WCW. Nanoparticle size and surface chemistry determine serum protein adsorption and macrophage uptake. J Am Chem Soc. 2012;134(4):2139–47.CrossRefGoogle Scholar
  46. 46.
    Roach P, Farrar D, Perry CC. Surface tailoring for controlled protein adsorption: effect of topography at the nanometer scale and chemistry. J Am Chem Soc. 2006;128(12):3939–45.CrossRefGoogle Scholar
  47. 47.
    Deng ZJ, Liang M, Toth I, Monteiro MJ, Minchin RF. Molecular interaction of poly(acrylic acid) gold nanoparticles with human fibrinogen. ACS Nano. 2012;6(10):8962–9.CrossRefGoogle Scholar
  48. 48.
    Tenzer S, Docter D, Kuharev J, Musyanovych A, Fetz V, Hecht R, et al. Rapid formation of plasma protein corona critically affects nanoparticle pathophysiology. Nat Nanotechnol. 2013;8(10):772–U1000.CrossRefGoogle Scholar

Copyright information

© The Regenerative Engineering Society 2018

Authors and Affiliations

  1. 1.Department of Biomedical EngineeringBen-Gurion University of the NegevBeer-ShevaIsrael
  2. 2.Department of Chemical EngineeringBen-Gurion University of the NegevBeer-ShevaIsrael

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