On the role of surface composition and curvature on biointerface formation and colloidal stability of nanoparticles in a protein-rich model system

Orts-Gil, Guillermo; Natte, Kishore; Thiermann, Raphael; Girod, Matthias; Rades, Steffi; Kalbe, Henryk; Thünemann, Andreas F.; Maskos, Michael; Österle, Werner

doi:10.1016/j.colsurfb.2013.02.027

Cited by 40 publications

(38 citation statements)

References 65 publications

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“…The protein-NP interaction is studied by incubating NPs in protein solutions for a period of time, either a single protein solution such as BSA, fibronectin and IgG, [11][12][13][14] or biological fluid containing multiple proteins such as serum, 15,16 plasma, cytosol, 17 fetal bovine serum (FBS), 18 fetal calf serum, synovial fluid, and cerebrospinal fluid. 19 Protein-NP complexes are then separated from the protein solution via instrumental analysis.…”

Section: Instrumental Analysis For Evaluating Protein Coronamentioning

confidence: 99%

“…18 Centrifugation is the typical method to collect NP-protein complex from the interaction media and loosely adsorbed proteins, and sucrose cushion centrifugation allows the separation of complex in a short time (30 sec). 11,12,22,23 The secondary structure of proteins can be evaluated by circular dichroism. However, this method cannot be used for a mixture of proteins due to its spectral complexity.…”

Section: Instrumental Analysis For Evaluating Protein Coronamentioning

confidence: 99%

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Protein corona: a new approach for nanomedicine design

Nguyen¹,

Lee²

2017

IJN

521

343

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After administration of nanoparticle (NP) into biological fluids, an NP–protein complex is formed, which represents the “true identity” of NP in our body. Hence, protein–NP interaction should be carefully investigated to predict and control the fate of NPs or drug-loaded NPs, including systemic circulation, biodistribution, and bioavailability. In this review, we mainly focus on the formation of protein corona and its potential applications in pharmaceutical sciences such as prediction modeling based on NP-adsorbed proteins, usage of active proteins for modifying NP to achieve toxicity reduction, circulation time enhancement, and targeting effect. Validated correlative models for NP biological responses mainly based on protein corona fingerprints of NPs are more highly accurate than the models solely set up from NP properties. Based on these models, effectiveness as well as the toxicity of NPs can be predicted without in vivo tests, while novel cell receptors could be identified from prominent proteins which play important key roles in the models. The ungoverned protein adsorption onto NPs may have generally negative effects such as rapid clearance from the bloodstream, hindrance of targeting capacity, and induction of toxicity. In contrast, controlling protein adsorption by modifying NPs with diverse functional proteins or tailoring appropriate NPs which favor selective endogenous peptides and proteins will bring promising therapeutic benefits in drug delivery and targeted cancer treatment.

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Section: Instrumental Analysis For Evaluating Protein Coronamentioning

confidence: 99%

Section: Instrumental Analysis For Evaluating Protein Coronamentioning

confidence: 99%

Protein corona: a new approach for nanomedicine design

Nguyen¹,

Lee²

2017

IJN

521

343

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“…Functionalization of nanosilica suspensions (starting from powdered nanosilica) by various agents has been investigated for toxicological evaluation, and their colloidal stability has been studied in either physiological media or biomimetic conditions. [20][21][22] Orts-Gil et al and Natte et al reported that the surface charge and hydrodynamic size of silica nanoparticles (Ludox TM50, Cat Number: 420778; Sigma-Aldrich Co., LLC, St Louis, MO, USA), changed depending on the concentration of ionic species, and that the silica nanoparticles with highly negative surface charge had colloidal stability at neutral or basic pH. 20,23 Industrial interests lie in two production classes for silica-based nanomaterials: fumed and colloidal.…”

Section: Introductionmentioning

confidence: 99%

Surface treatment of silica nanoparticles for stable and charge-controlled colloidal silica

An¹,

Kim²,

Kim³

et al. 2014

IJN

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An attempt was made to control the surface charge of colloidal silica nanoparticles with 20 nm and 100 nm diameters. Untreated silica nanoparticles were determined to be highly negatively charged and have stable hydrodynamic sizes in a wide pH range. To change the surface to a positively charged form, various coating agents, such as amine containing molecules, multivalent metal cation, or amino acids, were used to treat the colloidal silica nanoparticles. Molecules with chelating amine sites were determined to have high affinity with the silica surface to make agglomerations or gel-like networks. Amino acid coatings resulted in relatively stable silica colloids with a modified surface charge. Three amino acid moiety coatings (L-serine, L-histidine, and L-arginine) exhibited surface charge modifying efficacy of L-histidine > L-arginine > L-serine and hydrodynamic size preservation efficacy of L-serine > L-arginine > L-histidine. The time dependent change in L-arginine coated colloidal silica was investigated by measuring the pattern of the backscattered light in a Turbiscan™. The results indicated that both the 20 nm and 100 nm L-arginine coated silica samples were fairly stable in terms of colloidal homogeneity, showing only slight coalescence and sedimentation.

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“…[21][22] The formation of an opsonin corona would immediately alert the phagocyte system, 23 thereby promoting rapid clearance of the NPopsonins complex from the blood stream. Likewise, PEGylation of NPs has been used traditionally in vitro to reduce unspecific interactions with serum proteins, 11,[24][25][26] which typically results in a reduced uptake by cultured cells compared with uptake of their non-PEGylated counterparts. 27 That said, the formation of a protein corona can also hinder the interaction of NP ligands with the cellular membrane, resulting in a reduced uptake.…”

mentioning

confidence: 99%

Surface Functionalization of Nanoparticles with Polyethylene Glycol: Effects on Protein Adsorption and Cellular Uptake

et al. 2015

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Here we have investigated the effect of enshrouding polymer-coated nanoparticles (NPs) with polyethylene glycol (PEG) on the adsorption of proteins and uptake by cultured cells. PEG was covalently linked to the polymer surface to the maximal grafting density achievable under our experimental conditions. Changes in the effective hydrodynamic radius of the NPs upon adsorption of human serum albumin (HSA) and fibrinogen (FIB) were measured in situ using fluorescence correlation spectroscopy. For NPs without a PEG shell, a thickness increase of around 3 nm, corresponding to HSA monolayer adsorption, was measured at high HSA concentration. Only 50% of this value was found for NPs with PEGylated surfaces. While the size increase clearly reveals formation of a protein corona also for PEGylated NPs, fluorescence lifetime measurements and quenching experiments suggest that the adsorbed HSA molecules are buried within the PEG shell. For FIB adsorption onto PEGylated NPs, even less change in NP diameter was observed. In vitro uptake of the NPs by 3T3 fibroblasts was reduced to around 10% upon PEGylation with PEG chains of 10 kDa. Thus, even though the PEG coatings did not completely prevent protein adsorption, the PEGylated NPs still displayed a pronounced reduction of cellular uptake with respect to bare NPs, which is to be expected if the adsorbed proteins are not exposed on the NP surface.

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On the role of surface composition and curvature on biointerface formation and colloidal stability of nanoparticles in a protein-rich model system

Cited by 40 publications

References 65 publications

Protein corona: a new approach for nanomedicine design

Protein corona: a new approach for nanomedicine design

Surface treatment of silica nanoparticles for stable and charge-controlled colloidal silica

Surface Functionalization of Nanoparticles with Polyethylene Glycol: Effects on Protein Adsorption and Cellular Uptake

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