A Decade of the Protein Corona

Ke, Pu Chun; Lin, Sijie; Parak, Wolfgang J.; Davis, Thomas P.; Caruso, Frank

doi:10.1021/acsnano.7b08008

Cited by 493 publications

(420 citation statements)

References 20 publications

(30 reference statements)

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“…Their large size promotes extended circulation times and in the case of cancer treatment, they demonstrate passive tumor accumulation via the enhanced permeability and retention (EPR) effect . Furthermore, their high surface area can be functionalized with a broad range of moieties, making them ideal candidates for protein binding . Although the synthesis of sulfonated/sulfated polymeric NPs has already been explored, only one report exists on synthetic heparin‐mimicking NPs as growth factor stabilizers .…”

Section: Characterization Data For the Nanoparticles Used In Biologicmentioning

confidence: 99%

Heparin‐Mimicking Sulfonated Polymer Nanoparticles via RAFT Polymerization‐Induced Self‐Assembly

Gurnani

Bray

Richardson

et al. 2018

Macromol. Rapid Commun.

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Heparin plays a significant role in wound healing and tissue regeneration applications, through stabilization of fibroblast growth factors (FGF). Risks associated with batch-to-batch variability and contamination from its biological sources have led to the development of synthetic, highly sulfonated polymers as promising heparin mimics. In this work, a systematic study of an aqueous polymerization-induced self-assembly (PISA) of styrene from poly(2-acrylamido-2-methylpropane sodium sulfonate) (P(AMPS)) macro reversible addition-fragmentation chain transfer (macro-RAFT) agents produced a variety of spherical heparin-mimicking nanoparticles, which were further characterized with light scattering and electron microscopy techniques. None of the nanoparticles tested showed toxicity against mammalian cells; however, significant hemolytic activity was observed. Nonetheless, the heparin-mimicking nanoparticles outperformed both heparin and linear P(AMPS) in cellular proliferation assays, suggesting increased bFGF stabilization efficiencies, possibly due to the high density of sulfonated moieties at the particle surface.

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Section: Characterization Data For the Nanoparticles Used In Biologicmentioning

confidence: 99%

Heparin‐Mimicking Sulfonated Polymer Nanoparticles via RAFT Polymerization‐Induced Self‐Assembly

Gurnani

Bray

Richardson

et al. 2018

Macromol. Rapid Commun.

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“…To increase the targeting efficiency, the size, conformation, and surface properties of nanoparticles have been optimized . However, when nanoparticles flow through the bloodstream, they interact with various plasma proteins, leading to the formation of the protein layer on top of the particle surface, a process called protein corona . This protein‐corona formation influences the conformation and surface properties of nanoparticles and thus can significantly influence their circulating lifetime, cytotoxicity, body distribution, and endocytosis into specific cells, which may reduce the targeting efficiency .…”

Section: Introductionmentioning

confidence: 99%

“…However, when nanoparticles flow through the bloodstream, they interact with various plasma proteins, leading to the formation of the protein layer on top of the particle surface, a process called protein corona . This protein‐corona formation influences the conformation and surface properties of nanoparticles and thus can significantly influence their circulating lifetime, cytotoxicity, body distribution, and endocytosis into specific cells, which may reduce the targeting efficiency . To overcome this, nanoparticle surfaces have been often modified by attaching hydrophilic polymers (e.g., polyethylene glycol; PEGylation), but PEGylation induces the accelerated blood clearance and also cannot completely inhibit protein adsorption .…”

Section: Introductionmentioning

confidence: 99%

Effects of Nanoparticle Electrostatics and Protein–Protein Interactions on Corona Formation: Conformation and Hydrodynamics

Lee

2020

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All‐atom molecular dynamics simulations of plasma proteins (human serum albumin, fibrinogen, immunoglobulin gamma‐1 chain‐C, complement C3, and apolipoprotein A‐I) adsorbed onto 10 nm sized cationic, anionic, and neutral polystyrene (PS) particles in water are performed. In simulations of a single protein with a PS particle, proteins eventually bind to all PS particles, regardless of particle charge, in agreement with experiments showing the binding between anionic proteins and particles, which is further confirmed by calculating the binding free energies from umbrella sampling simulations. Simulations of mixtures of multiple proteins and a PS particle show the formation of the protein layer on the surface via the adsorption competition between proteins, which influences the binding affinity and structure of adsorbed proteins. In particular, diffusivities are much higher for proteins bound to the particle surface or to the boundary of the protein layer than for those bound to both the particle surface and other proteins, indicating the dependence of protein mobility on their positions in the layer. These findings help to explain in detail experimental observations regarding the replacement of plasma proteins at the early stage of corona formation and the difference in the binding strength of proteins in inner and outer protein‐layers.

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“…NP–protein interactions can vary considerably in strength, depending on the properties of the protein and NP surfaces. Weak binding results in a “soft corona,” characterized by fast dynamic exchange between adsorbed proteins and those in solution, whereas a tightly bound, “hard corona” is essentially persistent . Technically, hard coronae are easier to characterize because the NPs can be separated from the biofluid together with the adsorbed protein layer .…”

Section: Introductionmentioning

confidence: 99%

Formation of a Monolayer Protein Corona around Polystyrene Nanoparticles and Implications for Nanoparticle Agglomeration

Wang

Nienhaus

et al. 2019

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Nanoparticle (NP) interactions with cells and organisms are mediated by a biomolecular adsorption layer, the so‐called “protein corona.” An in‐depth understanding of the corona is a prerequisite to successful and safe application of NPs in biology and medicine. In this work, earlier in situ investigations on small NPs are extended to large polystyrene (PS) NPs of up to 100 nm diameter, using human transferrin (Tf) and human serum albumin (HSA) as model proteins. Direct NP sizing experiments reveal a reversibly bound monolayer protein shell (under saturating conditions) on hydrophilic, carboxyl‐functionalized (PS‐COOH) NPs, as was earlier observed for much smaller NPs. In contrast, protein binding on hydrophobic, sulfated (PS‐OSO3H) NPs in solvent of low ionic strength is completely irreversible; nevertheless, the thickness of the observed protein corona again corresponds to a protein monolayer. Under conditions of reduced charge repulsion (higher ionic strength), the NPs are colloidally unstable and form large clusters below a certain protein–NP stoichiometric ratio, indicating that the adsorbed proteins induce NP agglomeration. This comprehensive characterization of the persistent protein corona on PS‐OSO3H NPs by nanoparticle sizing and quantitative fluorescence microscopy/nanoscopy reveals mechanistic aspects of molecular interactions occurring during exposure of NPs to biofluids.

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A Decade of the Protein Corona

Cited by 493 publications

References 20 publications

Heparin‐Mimicking Sulfonated Polymer Nanoparticles via RAFT Polymerization‐Induced Self‐Assembly

Heparin‐Mimicking Sulfonated Polymer Nanoparticles via RAFT Polymerization‐Induced Self‐Assembly

Effects of Nanoparticle Electrostatics and Protein–Protein Interactions on Corona Formation: Conformation and Hydrodynamics

Formation of a Monolayer Protein Corona around Polystyrene Nanoparticles and Implications for Nanoparticle Agglomeration

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