Toward a Molecular Understanding of Nanoparticle-protein Interactions

Overview

Journal Biophys Rev

Publisher Springer

Specialty Biophysics

Date 2017 May 17

PMID 28510093

Citations 47

Authors

Lennart Treuel

Gerd Ulrich Nienhaus

Affiliations

Soon will be listed here.

Abstract

Wherever nanoparticles (NPs) come in contact with a living organism, physical and chemical interactions take place between the surfaces of the NPs and biomatter, in particular proteins. When NP are exposed to biological fluids, an adsorption layer of proteins, a "protein corona" forms around the NPs. Consequently, living systems interact with the protein-coated NP rather than with a bare NP. To anticipate biological responses to NPs, we thus require comprehensive knowledge of the interactions at the bio-nano interface. In recent years, a wide variety of biophysical techniques have been employed to elucidate mechanistic aspects of NP-protein interactions. In this brief review, we present the latest findings regarding the composition of the protein corona as it forms on NPs in the blood stream. We also discuss molecular aspects of this adsorption layer and its time evolution. The current state of knowledge is summarized, and issues that still need to be addressed to further advance our understanding of NP-protein interactions are identified.

Citing Articles

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References

Watari F, Takashi N, Yokoyama A, Uo M, Akasaka T, Sato Y . Material nanosizing effect on living organisms: non-specific, biointeractive, physical size effects. J R Soc Interface. 2009; 6 Suppl 3:S371-88. PMC: 2690091. DOI: 10.1098/rsif.2008.0488.focus. View

Pan Y, Neuss S, Leifert A, Fischler M, Wen F, Simon U . Size-dependent cytotoxicity of gold nanoparticles. Small. 2007; 3(11):1941-9. DOI: 10.1002/smll.200700378. View

Carpenter J, Randolph T, Jiskoot W, Crommelin D, Middaugh C, Winter G . Potential inaccurate quantitation and sizing of protein aggregates by size exclusion chromatography: essential need to use orthogonal methods to assure the quality of therapeutic protein products. J Pharm Sci. 2009; 99(5):2200-8. DOI: 10.1002/jps.21989. View

Treuel L, Malissek M, Gebauer J, Zellner R . The influence of surface composition of nanoparticles on their interactions with serum albumin. Chemphyschem. 2010; 11(14):3093-9. DOI: 10.1002/cphc.201000174. View

Service R . Science policy. Priorities needed for nano-risk research and development. Science. 2006; 314(5796):45. DOI: 10.1126/science.314.5796.45. View

Roach P, Farrar D, Perry C . Surface tailoring for controlled protein adsorption: effect of topography at the nanometer scale and chemistry. J Am Chem Soc. 2006; 128(12):3939-45. DOI: 10.1021/ja056278e. View

Gilbert B, Huang F, Zhang H, Waychunas G, Banfield J . Nanoparticles: strained and stiff. Science. 2004; 305(5684):651-4. DOI: 10.1126/science.1098454. View

Barnard A . Nanohazards: knowledge is our first defence. Nat Mater. 2006; 5(4):245-8. DOI: 10.1038/nmat1615. View

Shang L, Brandholt S, Stockmar F, Trouillet V, Bruns M, Nienhaus G . Effect of protein adsorption on the fluorescence of ultrasmall gold nanoclusters. Small. 2012; 8(5):661-5. DOI: 10.1002/smll.201101353. View

10.

Oberdorster G, Oberdorster E, Oberdorster J . Nanotoxicology: an emerging discipline evolving from studies of ultrafine particles. Environ Health Perspect. 2005; 113(7):823-39. PMC: 1257642. DOI: 10.1289/ehp.7339. View

11.

Rodriguez C, Fukuto J, Taguchi K, Froines J, Cho A . The interactions of 9,10-phenanthrenequinone with glyceraldehyde-3-phosphate dehydrogenase (GAPDH), a potential site for toxic actions. Chem Biol Interact. 2005; 155(1-2):97-110. DOI: 10.1016/j.cbi.2005.05.002. View

12.

Cedervall T, Lynch I, Foy M, Berggard T, Donnelly S, Cagney G . Detailed identification of plasma proteins adsorbed on copolymer nanoparticles. Angew Chem Int Ed Engl. 2007; 46(30):5754-6. DOI: 10.1002/anie.200700465. View

13.

Linse S, Cabaleiro-Lago C, Xue W, Lynch I, Lindman S, Thulin E . Nucleation of protein fibrillation by nanoparticles. Proc Natl Acad Sci U S A. 2007; 104(21):8691-6. PMC: 1866183. DOI: 10.1073/pnas.0701250104. View

14.

Aubin-Tam M, Hamad-Schifferli K . Gold nanoparticle-cytochrome C complexes: the effect of nanoparticle ligand charge on protein structure. Langmuir. 2005; 21(26):12080-4. DOI: 10.1021/la052102e. View

15.

Casals E, Pfaller T, Duschl A, Oostingh G, Puntes V . Time evolution of the nanoparticle protein corona. ACS Nano. 2010; 4(7):3623-32. DOI: 10.1021/nn901372t. View

16.

Jeong S, Kwon M, Lee E, Lee H, Cho S, Kim H . BiomarkerDigger: a versatile disease proteome database and analysis platform for the identification of plasma cancer biomarkers. Proteomics. 2009; 9(14):3729-40. DOI: 10.1002/pmic.200800593. View

17.

Wang T, Bai J, Jiang X, Nienhaus G . Cellular uptake of nanoparticles by membrane penetration: a study combining confocal microscopy with FTIR spectroelectrochemistry. ACS Nano. 2012; 6(2):1251-9. DOI: 10.1021/nn203892h. View

18.

BARON , Revault , ABADIE , Quiquampoix . Chymotrypsin Adsorption on Montmorillonite: Enzymatic Activity and Kinetic FTIR Structural Analysis. J Colloid Interface Sci. 1999; 214(2):319-332. DOI: 10.1006/jcis.1999.6189. View

19.

Cedervall T, Lynch I, Lindman S, Berggard T, Thulin E, Nilsson H . 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. PMC: 1892985. DOI: 10.1073/pnas.0608582104. View

20.

Matyus L, Szollosi J, Jenei A . Steady-state fluorescence quenching applications for studying protein structure and dynamics. J Photochem Photobiol B. 2006; 83(3):223-36. DOI: 10.1016/j.jphotobiol.2005.12.017. View