To miniaturize the assay into a 1536-well format amenable to qHTS, we chose MIA PaCa-2 and HT-29 because of their high levels of ALDH1A1. Utilizing the 8-step protocol described by Ming et al. as a starting point, we developed a “semi-automated” protocol described in S1 Table. Briefly, we plated 1,000 cells in a volume of 5 μL/well into black-optical quality clear bottom 1,536-well plates, and allowed cells to attach overnight. Culture media was subsequently removed by inverting and centrifuging plates using a plate adaptor as previously described and replaced with 5 μL of a solution of either 500 or 100 nM BAAA substrate in ALDEFLUOR buffer. To identify cells based on nuclear staining, we also included 0.5 nM Hoechst in the above buffer.
Computer simulations suggest that the contact ion pairing between the lipid head groups and the polycations’ ammonium groups leads to the formation of stable, albeit fragmented, lipid bilayer coronas. The mechanistic insight regarding lipid corona formation can be used to improve control over nano-bio interactions and to help understand why some nanomaterial-ligand combinations are detrimental to organisms but others are not. Engineered nanoparticles hold not only promise for technological innovation but also possible unforeseen risks for organisms upon inadvertent release into the environment. These insights help predict the impact that the increasingly widespread use of engineered nanomaterials has on their fate once they enter the food chain, which many of them may eventually do. Here, we provide evidence for spontaneous lipid corona formation that engenders new particle properties without the need for active mixing upon attachment to stationary and suspended lipid bilayer membranes. The mechanism of lipid corona formation can be used to improve control over nano-bio interactions and to help understand why some nanomaterial-ligand combinations are detrimental to organisms but others are not.
PCN complexes illustrate much slower kinetics of adsorption due to a smaller diffusion coefficient according to their larger size. The free proteins available in the solution were estimated considering early-time values of the dynamic surface tension, used for estimation of the adsorbed proteins per unit area of the silica surface (mol/cm²), considering the initial protein concentration in the bulk. The results show very good agreement with others’ results provided by AFM, DLS, UV–vis Spectroscopy, Multi-Parametric Surface Plasmon Resonance (MP-SPR), and Quartz Crystal Microbalance . The measured interfacial elasticity values confirm PCN formation and provides additional information for better differentiations of the corona layers.
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Initial experiments used a model system composed of polystyrene NPs functionalized with either amine or carboxylate groups to provide a cationic or anionic surface, respectively. Serum proteins adsorb onto the surface of both cationic and anionic NPs, forming a net anionic protein-NP complex. Although these protein-NP complexes have similar diameters and effective surface charges, they show the exact opposite behavior in terms of cellular binding. In the presence of bovine serum albumin , the cellular binding of BSA-NP complexes formed from cationic NPs is enhanced, whereas the cellular binding of BSA-NP complexes formed from anionic NPs is inhibited. Similar results were obtained for anionic quantum dots and colloidal gold nanospheres. Using competition assays, we determined that BSA-NP complexes formed from anionic NPs bind to albumin receptors on the cell surface.
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These experiments demonstrate that magnetic separation could be used for any type of nanoparticle in which a magnetic core can be embedded. Higher-throughput corona characterization will also require lower-cost approaches to proteomics. We report a comparison of fast, low-cost, and standard, slower, higher-cost liquid chromatography coupled with mass spectrometry to identify the protein corona. These methods will provide select the correct statement contrasting gametophytes and sporophytes. a step forward in the acquisition of the large datasets necessary to predict nanoparticle-protein interactions. Our goal was to understand how this protein layer affected cellular-level events, including NP binding, internalization, and transport. A combination of microscopy, which provides spatial resolution, and spectroscopy, which provides molecular information, is necessary to probe protein-NP-cell interactions.
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