Adsorption of a Protein Monolayer via Hydrophobic Interactions Prevents Nanoparticle Aggregation under Harsh Environmental Conditions

Domínguez-Medina, Sergio; Blankenburg, Jan; Olson, Jana; Landes, Christy F.; Link, Stephan

doi:10.1021/sc400042h

Cited by 172 publications

(160 citation statements)

References 79 publications

Supporting

Mentioning

144

Contrasting

Unclassified

Order By: Relevance

“…[81][82][83] Conversely, in several studies, the adsorption of proteins onto NPs also improves NP stability and prevents formation of NP aggregates. 84,85 Therefore, the protein corona can adjust the average size of NPs and may change the cellular uptake pathway and biodistribution.…”

Section: Targeting Purposementioning

confidence: 99%

Protein corona: a new approach for nanomedicine design

Nguyen¹,

Lee²

2017

IJN

536

343

View full text Add to dashboard Cite

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.

show abstract

Section: Targeting Purposementioning

confidence: 99%

Protein corona: a new approach for nanomedicine design

Nguyen¹,

Lee²

2017

IJN

536

343

View full text Add to dashboard Cite

show abstract

“…Serum albumin is the most abundant protein component in blood plasma. Bovine serum albumin (BSA) is often selected as a model protein to study nanoparticle-protein interactions, because it shares 98% of its amino acid sequence with its human variant (Dominguez-Medina et al, 2013).…”

Section: Introductionmentioning

confidence: 99%

Effects of humic acid and bovine serum albumin on the agglomeration and sedimentation of oxide nanoparticles

Lin

Chen

et al. 2014

J. Zhejiang Univ. Sci. A

View full text Add to dashboard Cite

Abstract:To better understand the nanoparticle (NP) transport in the environment, the agglomeration and sedimentation of Al 2 O 3 , SiO 2 , and TiO 2 NPs were evaluated after being treated with bovine serum albumin (BSA) and a commercial humic acid (HA). The morphology of NP agglomerates was examined through a transmission electron microscope (TEM), and the agglomeration kinetics was evaluated using established time-resolved dynamic light scattering techniques. BSA treatments decreased the hydrodynamic diameters (d H ) of the three NPs in both NaCl and CaCl 2 electrolytes due to their steric repulsive forces caused by the BSA globular architecture. The treatments using HA induced the smallest d H of NPs in NaCl electrolyte, but the largest d H of NPs was found in CaCl 2 electrolyte, because the HA bound to each other via calcium complexation and thereby enhanced the NP agglomeration. The zeta potentials of NPs were not the dominant factor to affect agglomeration. The NP sedimentation kinetics were studied through measuring the suspension optical absorbance. It was shown that the BSA treatments retarded the sedimentation in most situations; however, HA treatments accelerated the sedimentation greatly in CaCl 2 electrolyte, which was consistent with the measured changes in the d H values. The smallest d H of HA-treated NPs in NaCl electrolyte did not result in the lowest sedimentation rate, which indicated that the agglomeration size was not the only factor to affect the NP sedimentation.

show abstract

“…Due to their outstanding optical properties, an increasing number of studies have focused on Au for a wide range of biological and biomedical applications such as biosensing, biomedical imaging, gene and drug delivery, or disease detection [55,56]. Tables 1 and 2 summarize typical NPs, organized by the main analytical method used to characterize them in a variety of [28] Ag NPs (Bare and polysaccharide coated) Alveolar and lysosomal fluid Stability and aggregation Casals (2010) [59] Au NPs Complete cell media Evolution of protein corona Casals (2011) [60] Au and Ag NPs Complete cell media Protein corona formation and biological implications Cho (2011) [9] Au NPs (bare and PEG coated) Complete cell media Influence of sedimentation and diffusion on cellular uptake De Paoli Lacerda (2010) [61] Au NPs Protein solutions Interaction of NPs with human blood proteins Dominguez-Medina (2013) [62] Au NPs (citrate coated) PBS and BSA solutions Synthesis of advanced NPs to prevent aggregation Fatisson (2012) [63] Au NPs Complete cell media Impact of cell culture media components on stability Hühn (2013) [64] Au NPs (negatively and positively charged polymers)…”

Section: Characterization Of Nps In Physiological Fluidsmentioning

confidence: 99%

“…It has been repeatedly shown that the degree of aggregation has an impact on cellular response [70,77] and much effort is dedicated to improve the stability of NPs in such media [76]. Although it has been demonstrated that protein adsorption can generally stabilize the system [62,68,71], surface-charge dependent interactions must be also considered [64]; characterizing the extent and time evolution of protein adsorption may bring further insights [60,72]. Other studies have used the method to study kinetics of aggregation and dissolution of e.g.…”

Section: Scatteringmentioning

confidence: 99%

“…However, as soon as NP-protein complexation occurs, this approach should not be followed, as the 'reference scattering' from the protein alone is not valid anymore. In this regard depolarized scattering provides a promising alternative to characterize NP in physiological fluids, which relies on the optical anisotropy of even spherical plasmonic NPs [79], which either stems from shape and/or from internal [62] Au NPs (citrate coated) PBS and BSA solutions Synthesis of advanced NPs to prevent aggregation Garcia (2015) [95] Au nanorods and spheres (glycan and PEG-coated) 10% FBS in PBS and DMEM Stability and targeting in protein rich media Pyshnaya (2014) [75] Au nanorods and spheres (PEI and BSA coated) DMEM containing 10% FBS Impact of physiological fluids on size and stability McCuspie (2011) [96] Ag NPs (BSA coated) Synthetic lung fluid Dispersion stabilization of NPs and effect on colloidal stability Jenkins (2015) [81] Au NPs (citrate coated) Blood Monitoring LSPR for aggregation studies Kah (2014) [97] Au nanorods (amphi-philic ligands coating) anisotropy. It has been shown that, compared to plasmonic NPs, scattering of depolarized light from the physiological fluid is weak, and thus, excellent 'contrast' with an essentially zero background can be obtained [58].…”

Section: Scatteringmentioning

confidence: 99%

See 1 more Smart Citation