Tumor necrosis factor interaction with gold nanoparticles

Tsai, De-Hao; Elzey, Sherrie; DelRio, Frank W.; Keene, Athena M.; Tyner, Katherine M.; Clogston, Jeffrey D.; MacCuspie, Robert I.; Guha, Sudipto; Zachariah, Michael R.; Hackley, Vincent A.

doi:10.1039/c2nr30415e

Cited by 44 publications

(38 citation statements)

References 74 publications

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“…4B). This result indicated that some of the untreated unlabeled TNFα had dissociated to the monomeric form during the analysis, as has been reported previously with SDS-PAGE analysis [29, 30]. However, cross-linked unlabeled TNFα showed a single band at the trimer location (Fig.…”

Section: Resultssupporting

confidence: 86%

Transport and binding of tumor necrosis factor-α in articular cartilage depend on its quaternary structure

Byun¹,

Sinskey²,

Lu³

et al. 2013

Archives of Biochemistry and Biophysics

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The effect of tumor necrosis factor-α (TNFα) on cartilage matrix degradation is mediated by its transport and binding within the extracellular matrix (ECM) of the tissue, which mediates availability to cell receptors. Since the bioactive form of TNFα is a homotrimer of monomeric subunits, conversion between trimeric and monomeric forms during intratissue transport may affect binding to ECM and, thereby, bioactivity within cartilage. We studied the transport and binding of TNFα in cartilage, considering the quaternary structure of this cytokine. Competitive binding assays showed significant binding of TNFα in cartilage tissue, leading to an enhanced uptake. However, studies in which TNFα was cross-linked to remain in the trimeric form revealed that the binding of trimeric TNFα was negligible. Thus, binding of TNFα to ECM was associated with the monomeric form. Binding of TNFα was not disrupted by pre-treating cartilage tissue with trypsin, which removes proteoglycans and glycoproteins but leaves the collagen network intact. Therefore, proteoglycan loss during osteoarthritis should only alter the passive diffusion of TNFα but not its binding interaction with the remaining matrix. Our results suggest that matrix binding and trimer-monomer conversion of TNFα both play crucial roles in regulating the accessibility of bioactive TNFα within cartilage.

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Section: Resultssupporting

confidence: 86%

Transport and binding of tumor necrosis factor-α in articular cartilage depend on its quaternary structure

Byun¹,

Sinskey²,

Lu³

et al. 2013

Archives of Biochemistry and Biophysics

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“…Because NPs have high surface free energy, in order to decrease NP surface energy [51], many kinds of protein can be adsorbed on the surface of Au NPs with distinct binding affinities [52, 53]. When exposed to biological fluids or microenvironments, Au NPs can contact and adsorb a variety of proteins such as ubiquitin [54, 55], serum albumin [56, 57], tumor necrosis factor [58, 59], cytochrome C [29], fibrinogen [60], or polypeptides [61]. Usually, the high abundance proteins first arrive at and adsorb on the surface of NPs, but they will be eventually replaced by high-affinity proteins to form NP–protein complexes [62].…”

Section: Au Np–protein Interactionsmentioning

confidence: 99%

Interaction of gold nanoparticles with proteins and cells

Wang

et al. 2015

Science and Technology of Advanced Materials

167

117

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Gold nanoparticles (Au NPs) possess many advantages such as facile synthesis, controllable size and shape, good biocompatibility, and unique optical properties. Au NPs have been widely used in biomedical fields, such as hyperthermia, biocatalysis, imaging, and drug delivery. The broad application range may result in hazards to the environment and human health. Therefore, it is important to predict safety and evaluate therapeutic efficiency of Au NPs. It is necessary to establish proper approaches for the study of toxicity and biomedical effects. In this review, we first focus on the recent progress in biological effects of Au NPs at the molecular and cellular levels, and then introduce key techniques to study the interaction between Au NPs and proteins. Knowledge of the biomedical effects of Au NPs is significant for the rational design of functional nanomaterials and will help predict their safety and potential applications.

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“…Recent evidence suggests that proteins adsorbed to surfaces aggregate [147,148]. Since these aggregated proteins may then desorb, one might reasonably wonder, how these desorbing 74 proteins may impact size distributions obtained with ES-DMA, an aspect that has never been studied before.…”

Section: Introductionmentioning

confidence: 99%

Electrospray–differential mobility analysis of bionanoparticles

Guha

Tarlov

et al. 2012

Trends in Biotechnology

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The growth of the multibillion dollar bionanoparticle industry has spurred the development of new physical characterization methods. One such method, electrospraydifferential mobility analysis (ES-DMA) constitutes an electrospray for aerosolization of bionanoparticles (such as viruses, gold-nanoparticles, proteins, nanoparticle-protein complexes) and an ion mobility method that operates at atmospheric conditions, and separates bionanoparticles spatially. This dissertation identifies some relevant "problem" areas for ES-DMA by reviewing selected applications.Some such problems are: proteins while passing through ES capillaries are found to interact with it and thus produce time dependent size distributions. Further, it is thought that adsorbed proteins may subsequently desorb and influence size distributions with the ES-DMA which may concomitantly affect quantification of aggregates. These artifacts are studied systematically and it is demonstrated that ES-DMA can quantify adsorption-desorption of complex protein mixtures at high shear rates. Further, it is shown that desorbing proteins do not have a significant effect on size distributions. Another artifact of the ES takes place during the aersolization process. Two units (called monomers) of a bionanoparticle may get encapsulated in the same ES droplet and upon drying of the droplet create artificial dimers thus affecting quantification with ES-DMA. Assuming Poisson distribution, this thesis provides a systematic approach that can be undertaken to eliminate this artifact. A third artifact arises from the low sensitivity of the DMA to size increase. When a ligand (for e.g. protein) adsorbs to a bionanoparticle it creates an increase in the size of the later, which can be used to quantify the amount of ligand adsorbed per bionanoparticle. As ligands can change conformations upon adsorption, using ES-DMA for such applications may be flawed. This issue has been identified and a solution has been provided by integrating a mass analyzer after the ES-DMA.After correcting for these artifacts, this dissertation delves into characterization of different types of bionanoparticles and demonstrates that ES-DMA has several advantages over other traditional techniques such as transmission electron microscopy, size exclusion chromatography, analytical ultracentrifugation, dynamic light scattering and plaque assay and thus has immense potential to become a process analytical technique in biomanufacturing environments. ELECTROSPRAY-DIFFERENTIAL MOBILITY ANALYSIS OF BIONANOPARTICLES

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Tumor necrosis factor interaction with gold nanoparticles

Cited by 44 publications

References 74 publications

Transport and binding of tumor necrosis factor-α in articular cartilage depend on its quaternary structure

Transport and binding of tumor necrosis factor-α in articular cartilage depend on its quaternary structure

Interaction of gold nanoparticles with proteins and cells

Electrospray–differential mobility analysis of bionanoparticles

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