Nanoparticles with decreasing surface hydrophobicities: influence on plasma protein adsorption

Gessner, Andrea; Waicz, R; Lieske, Antje; Paulke, Bernd-Reiner; Mäder, Karsten; Müller, Rainer H.

doi:10.1016/s0378-5173(99)00432-9

Cited by 322 publications

(219 citation statements)

References 8 publications

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“…[insert Figure 2 about here] It is known that protein adsorption is depending on the hydrophobicity of the particle surface [29][30][31]. As stated previously, 90 wt% of ALF are (phospho)lipids and we probably washed out this lipid fraction into our pBALF at least partially.…”

Section: Particle Propertiesmentioning

confidence: 70%

Interaction of metal oxide nanoparticles with lung surfactant protein A

Schulze

Schaefer

Ruge

et al. 2011

European Journal of Pharmaceutics and Biopharmaceutics

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Section: Particle Propertiesmentioning

confidence: 70%

Interaction of metal oxide nanoparticles with lung surfactant protein A

Schulze

Schaefer

Ruge

et al. 2011

European Journal of Pharmaceutics and Biopharmaceutics

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“…A central methodological problem is to separate free protein from protein bound to nanoparticles, ideally employing nonperturbing methods that do not disrupt the protein-particle complex or induce additional protein binding. The preferred method to-date has been centrifugation, identifying the major serum proteins albumin, IgG and fibrinogen as being associated with a wide range of particles of seemingly disparate molecular composition (5)(6)(7)(8)(9)(10)(11)(12)(13)(14)(15)(16)(17)(18). Due to its high abundance, albumin is almost always observed on particles and may be retrieved even if it has relatively low affinity.…”

mentioning

confidence: 99%

Understanding the nanoparticle–protein corona using methods to quantify exchange rates and affinities of proteins for nanoparticles

Cedervall¹,

Lynch²,

Lindman

et al. 2007

Proc. Natl. Acad. Sci. U.S.A.

2,802

2,561

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Due to their small size, nanoparticles have distinct properties compared with the bulk form of the same materials. These properties are rapidly revolutionizing many areas of medicine and technology. Despite the remarkable speed of development of nanoscience, relatively little is known about the interaction of nanoscale objects with living systems. In a biological fluid, proteins associate with nanoparticles, and the amount and presentation of the proteins on the surface of the particles leads to an in vivo response. Proteins compete for the nanoparticle ''surface,'' leading to a protein ''corona'' that largely defines the biological identity of the particle. Thus, knowledge of rates, affinities, and stoichiometries of protein association with, and dissociation from, nanoparticles is important for understanding the nature of the particle surface seen by the functional machinery of cells. Here we develop approaches to study these parameters and apply them to plasma and simple model systems, albumin and fibrinogen. A series of copolymer nanoparticles are used with variation of size and composition (hydrophobicity). We show that isothermal titration calorimetry is suitable for studying the affinity and stoichiometry of protein binding to nanoparticles. We determine the rates of protein association and dissociation using surface plasmon resonance technology with nanoparticles that are thiol-linked to gold, and through size exclusion chromatography of protein-nanoparticle mixtures. This method is less perturbing than centrifugation, and is developed into a systematic methodology to isolate nanoparticle-associated proteins. The kinetic and equilibrium binding properties depend on protein identity as well as particle surface characteristics and size.

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“…This loose division into hard and soft coronas has been illustrated in some examples (1,2) in which a simple method of ''pelleting'' (spinning particles and medium, removing the supernatant, and then washing the pellet to discard loosely associated molecules) is found to be consistent with the identification of the hard corona via other techniques. This method must be applied with care (2), because the washing steps can fail to remove excess (abundant) unbound proteins, but it has been applied with some success (3)(4)(5)(6)(7). Several investigations of the protein corona around polystyrene particles have used silver-stained 2D PAGE gels to detect the proteins eluted from the particles followed by spot excision, trypsin digestion, and peptide detection with mass spectrometry (3)(4)(5)(6)(7).…”

mentioning

confidence: 99%

Nanoparticle size and surface properties determine the protein corona with possible implications for biological impacts

Lundqvist

Stigler

Elia

et al. 2008

Proc. Natl. Acad. Sci. U.S.A.

2,680

2,340

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Nanoparticles in a biological fluid (plasma, or otherwise) associate with a range of biopolymers, especially proteins, organized into the ''protein corona'' that is associated with the nanoparticle and continuously exchanging with the proteins in the environment. Methodologies to determine the corona and to understand its dependence on nanomaterial properties are likely to become important in bionanoscience. Here, we study the long-lived (''hard'') protein corona formed from human plasma for a range of nanoparticles that differ in surface properties and size. Six different polystyrene nanoparticles were studied: three different surface chemistries (plain PS, carboxyl-modified, and amine-modified) and two sizes of each (50 and 100 nm), enabling us to perform systematic studies of the effect of surface properties and size on the detailed protein coronas. Proteins in the corona that are conserved and unique across the nanoparticle types were identified and classified according to the protein functional properties. Remarkably, both size and surface properties were found to play a very significant role in determining the nanoparticle coronas on the different particles of identical materials. We comment on the future need for scientific understanding, characterization, and possibly some additional emphasis on standards for the surfaces of nanoparticles.bionanoscience ͉ mass spectrometry ͉ interactions ͉ proteomics ͉ human plasma

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Nanoparticles with decreasing surface hydrophobicities: influence on plasma protein adsorption

Cited by 322 publications

References 8 publications

Interaction of metal oxide nanoparticles with lung surfactant protein A

Interaction of metal oxide nanoparticles with lung surfactant protein A

Understanding the nanoparticle–protein corona using methods to quantify exchange rates and affinities of proteins for nanoparticles

Nanoparticle size and surface properties determine the protein corona with possible implications for biological impacts

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