The on-bead digestion of protein corona on nanoparticles by trypsin immobilized on the magnetic nanoparticle

Hu, Zhengyan; Zhao, Liang; Zhang, Hongyan; Zeng, Yi; Wu, Ren’an; Zou, Hanfa

doi:10.1016/j.chroma.2014.01.077

Cited by 22 publications

(12 citation statements)

References 37 publications

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“…Using the immobilized magnetic trypsin, the human plasma protein coronas on Fe 3 O 4 nanoparticles only with the size different from 30 to 250 nm though possessing the same chemical property and surface zeta potential were efficiently identified with the distinction of different abundant proteins. Hu et al [51,52] demonstrated that particle size was one of the critical factors which influenced the formation of human plasma protein corona on Fe 3 O 4 nanoparticles. This hints the impact of the nanoparticle size on biobehaviors and fates of Fe 3 O 4 nanoparticles when they enter into a biological system.…”

Section: Proteomic Identification Of Protein Corona By Liquid Chromatmentioning

confidence: 98%

“…Additionally, the self-digestion of the applied free trypsin in solution would bring interference towards the identification of protein corona by mass spectrometry and the subsequent protein database search. As immobilized trypsin exhibits the high efficiency and the reduced self-digestion for protein digestion [49,50], Hu et al [51] further developed a protocol of the on-beads digestion with the immobilized trypsin on the magnetic nanoparticle. Wherein, the immobilized trypsin on the magnetic Fe 3 O 4 nanoparticle was developed to cleave the adsorbed proteins from the surface of nanoparticles ( Figure 5).…”

Section: Proteomic Identification Of Protein Corona By Liquid Chromatmentioning

confidence: 99%

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Proteomic profiling of protein corona formed on the surface of nanomaterial

Zhang

2015

Sci. China Chem.

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The formation of protein coronas on nanomaterial will significantly alter the surface properties of nanomaterial in biological systems and subsequently impact biological responses including signaling, cellular uptake, transport, and toxicity etc. It is of critical importance to understand the formation of protein coronas on the surface of nanomaterial. Analytical techniques, especially mass spectrometry-based proteomics methods, are playing a key role for the qualitative and quantitative analyses of protein coronas on nanomaterial. In this review, the proteomic approaches developed for the characterization of protein coronas on various nanomaterials are introduced with the emphasis on the mass spectrometry-based proteomic strategies.protein corona, nanomaterial, proteomics, mass spectrometry, identification and quantification, gel electrophoresis

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Section: Proteomic Identification Of Protein Corona By Liquid Chromatmentioning

confidence: 98%

Section: Proteomic Identification Of Protein Corona By Liquid Chromatmentioning

confidence: 99%

Proteomic profiling of protein corona formed on the surface of nanomaterial

Zhang

2015

Sci. China Chem.

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“…When NPs are administered in biological systems they interact with the components present in the physiological environment [1], being exposed to species of biomolecules and substances that result in the formation of the biological corona [10]. The complexes formed by the interaction of NPs and proteins form the biological component of the protein corona (PC) [1,[11][12][13][14], which has a dynamic composition defined by complex interactions that depend on colloidal forces, as well as dynamic physicochemical characteristics of the particle [10,14]. PC formation induces changes in the nature of the extracellular matrix of the NP, altering the original biological identity [7,10,11,15].…”

Section: Introductionmentioning

confidence: 99%

“…The complexes formed by the interaction of NPs and proteins form the biological component of the protein corona (PC) [1,[11][12][13][14], which has a dynamic composition defined by complex interactions that depend on colloidal forces, as well as dynamic physicochemical characteristics of the particle [10,14]. PC formation induces changes in the nature of the extracellular matrix of the NP, altering the original biological identity [7,10,11,15]. In this context, the adsorbed proteins control the cellular interaction receptors, coordinate the internalization pathway and modulate the immune response, such as the macrophage uptake, complement system activation and cellular toxicity [10,11,14,16,17].…”

Section: Introductionmentioning

confidence: 99%

Formation of Protein Corona on Rhodium Citrate-Functionalized Magnetic Nanoparticles and Their Interaction with Human Macrophages

Lago¹,

Carvalho²,

Chaves³

et al. 2019

J Nanomed Nanotechnol

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Nanoscience and Nanotechnology enable innovations for Medicine and for Biomedical Science. Among the current nanoparticles, maghemite associated with rhodium citrate (Magh-RhCit) has been shown to be promising, because it reduces side effects of drugs while maintaining cytotoxicity for tumor cells. However, NPs in contact with biological fluids are immediately coated by proteins (protein corona) that are unique to each nanomaterial. In this study, the adsorption of the most abundant binding proteins was studied in vitro using a three-step analysis: (1) characterization of the magnetic fluid (Magh-RhCit) before and after incubation with serum; (2) identification and physical and biochemical analysis of protein corona; and (3) the cellular internalization of these nanoparticles in human macrophages. Magh-RhCit was initially obtained in the magnetite phase (Fe 3 O 4) via alkaline coprecipitation of Fe 2+ and Fe 3+ ions and subsequently oxidized to maghemite by the bubbling of oxygen gas in the suspension. Later, rhodium citrate was associated with nanoparticles. Dynamic Light Scattering data were used for characterization of the hydrodynamic diameter and zeta potential. The morphological characterization and measurement of the particles were obtained from Scanning and Transmission Electron Microscopy, and the X-ray Diffraction technique. The identification of the proteins was performed by Liquid Chromatograph coupled to Mass Spectrometry. Human blood serum altered the characteristics of the nanoparticle, making it less polydisperse, larger and with less negative zeta potential, indicating the formation of the protein corona. Forty-nine proteins (which mostly promote opsonization, phagocytosis and endocytosis in cells of the immune system) were identified and characterized: albumin, IgGs, apoliproteins, serpins, complement (C5), kinases, haptoglobin, glycoproteins and transferrin. Nanoparticle characterization and mass spectrometric data of the digested protein corona suggest improved biocompatibility. Moreover, results regarding nanoparticles' interaction with macrophages suggest that the corona may have profoun implications for in vitro and in vivo extrapolations and will require some consideration in the future.

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“…Nanoplatform which combined the inorganic-organic composite together fills the gap by its prominent advantages in complementation and cooperatives in multifunction. As for inorganic composite, magnetic nanoparticles provide us an environmental friendly way of separation and recycle [31][32][33]. There are different ways in ion detection and removal based on the functionalized magnetic nanoplatform.…”

Section: Introductionmentioning

confidence: 99%

Rhodamine Derivative Functionalized Magnetic Nanoplatform for Cu²⁺ Sensing and Removal

Wang

Tian³

et al. 2018

Journal of Nanomaterials

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Pollution caused by copper is one of the key factors of environment contamination. As one of the heavy metals, copper is hard to decompose in nature; the biological enrichment of which may lead to severe damage to health. Cu2+ detection, thus, possesses a bright application prospect both in environment protection and in human health. In this paper, a dual-functional fluorescence-magnetic composite nanoplatform has been designed to sensitively detect, meanwhile, capture, and remove Cu2+ in the solution of water and ethanol (1 : 1, v/v). The core-shell structure nanoparticle synthesized by using Fe3O4 as core and SiO2 as shell is covalently bonded with rhodamine derivatives on the silica layer to construct the nanoplatform. The emission is increased upon the addition of Cu2+, showing fluorescence turn on effect for the detection, and the limit of detection is as low as 1.68 nM. Meanwhile, Cu2+ ions are captured by the coordination with rhodamine derivatives and can be removed with the help of magnetic field.

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The on-bead digestion of protein corona on nanoparticles by trypsin immobilized on the magnetic nanoparticle

Cited by 22 publications

References 37 publications

Proteomic profiling of protein corona formed on the surface of nanomaterial

Proteomic profiling of protein corona formed on the surface of nanomaterial

Formation of Protein Corona on Rhodium Citrate-Functionalized Magnetic Nanoparticles and Their Interaction with Human Macrophages

Rhodamine Derivative Functionalized Magnetic Nanoplatform for Cu²⁺ Sensing and Removal

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The on-bead digestion of protein corona on nanoparticles by trypsin immobilized on the magnetic nanoparticle

Cited by 22 publications

References 37 publications

Proteomic profiling of protein corona formed on the surface of nanomaterial

Proteomic profiling of protein corona formed on the surface of nanomaterial

Formation of Protein Corona on Rhodium Citrate-Functionalized Magnetic Nanoparticles and Their Interaction with Human Macrophages

Rhodamine Derivative Functionalized Magnetic Nanoplatform for Cu2+ Sensing and Removal

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Product

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Rhodamine Derivative Functionalized Magnetic Nanoplatform for Cu²⁺ Sensing and Removal