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Order Picornavirales
Published in Paul Pumpens, Peter Pushko, Philippe Le Mercier, Virus-Like Particles, 2022
Paul Pumpens, Peter Pushko, Philippe Le Mercier
Somasundaram et al. (2016) presented obstacles for the enhanced production of both EV71 and CVA16 VLPs, comparing the VLP yields in Sf9 and HighFive cells. The authors used high-resolution asymmetric flow field-flow fractionation couple with multiangle light scattering (AF4-MALS) for the first time to characterize the EV71 and CVA16 VLPs, displaying an average root mean square radius of 15 ± 1 nm and 15.3 ± 5.8 nm, respectively.
Physiology and Growth
Published in Paul Pumpens, Single-Stranded RNA Phages, 2020
The flow field-flow fractionation (FFF), was applied for the separation and purification of the phage Qβ as a model, although the phages f2 and MS2 were also involved in the study (Giddings et al. 1977). The forced-flow electrophoresis (FFE), was developed later with the use of the phage MS2, among other phages, to characterize the separation process (Mullon et al. 1987).
Identifying Nanotoxicity at the Cellular Level Using Electron Microscopy
Published in Suresh C. Pillai, Yvonne Lang, Toxicity of Nanomaterials, 2019
Kerry Thompson, Alanna Stanley, Emma McDermott, Alexander Black, Peter Dockery
Adequate quantification of nanoparticles in cells and tissues is becoming established as an essential element in studies of nanoparticle toxicology. Estimating the cellular dose helps in the assessment of both the effect of and possible risk from nanomaterials (Elsaesser and Howard, 2012). The wide range of microscopical and analytical methods that have been deployed in nanoparticle research studies include light microscopy (Huang et al., 2002, Alivisatos et al., 2005), electron microscopy (Muhlfeld et al., 2007a, Nativo et al., 2008), stereology (Brandenberger et al., 2010b), radioactive labelling (Jani et al., 1990, Kreyling et al., 2009), magnetic nanoparticle labelling (Sun et al., 2008, 2010), mass spectrometry (Chithrani et al., 2006, Gojova et al., 2007) and field flow fractionation (Deering et al., 2008).
Liposome: composition, characterisation, preparation, and recent innovation in clinical applications
Published in Journal of Drug Targeting, 2019
Kamel S. Ahmed, Saied A. Hussein, Abdelmoneim H. Ali, Sameh A. Korma, Qiu Lipeng, Chen Jinghua
As a result of the drawbacks of the electron microscope technique (EM) (TEM, cryo-EM, freeze fracture TEM) like complicated sample preparation (staining and drying procedures), induce shape alteration and shrinkage, and time-consuming, so atomic force microscopy (AFM) is a novel rapid techniques that are able to assess the three-dimensional shape of the liposome surface without sample modification with a sharp probe or tip, and doesn't cause any damaging or alteration effects on the liposome, but liposome dispersion analysis should be immediately after deposition of the sample because evaporation of the aqueous medium will lead to vesicles rearrangements. Field-flow fractionation (FFF) is a flexible elution method, provides convenient and rapid procedures for measurement and separation of liposome size. It has the ability to separate a wide range (1 nm – 100 µm) of particle sizes with high resolution. In this technique particle size separation is carried out depending on hydrodynamic size basis (flow FFF) or weight basis (sedimentation FFF). Furthermore, when joined to other detectors like light scattering, transmission electron microscopy, UV-absorbance, and atomic force microscopy can offer a proper information on vesicle properties such as size, structural parameters, shape, and sample contamination [51,57].
Unraveling the complexity of the extracellular vesicle landscape with advanced proteomics
Published in Expert Review of Proteomics, 2022
Julia Morales-Sanfrutos, Javier Munoz
Affinity-based strategies exploit specific interactions between EVs surface markers with antibodies, molecules, and functional groups immobilized onto a variety of solid supports (e.g. magnetic or agarose beads, plates, monolithic columns). Antibodies targeting tetraspanin family proteins, such as CD9, CD63, and CD81, are commonly used for the immune-purification of sEVs, as there are several ready-to-use kits commercially available. Additionally, other antibodies have been used for the isolation of sEVs, for example, annexin, EpCAM, or A33 [38]. Besides immunoaffinity methods, other strategies have been used for isolating different EV populations. Ghosh et al [39]. described the potential of Veneceremin (Vn), a synthetic peptide that specifically binds to heat shock proteins (HSPs), for isolation of sEVs from cell culture media and other body fluids. The affinity of lectins for glycoproteins, present on the vesicle surface, has been also exploited for sEVs isolation [40]. One of the main advantages of immunoaffinity is that it can provide high sEVs purity compared to other approaches [41]. This enables purifying specific sEVs subpopulations, which is essential for understanding EVs biology [42]. Nonetheless, this selectivity can be an issue when the aim of the study is the general sEVs population. It should be highlighted that, in many cases, this strategy requires pre-enrichment step to remove contaminants that bind the resin/antibody in an unspecific manner or to reduce the sample volume.(7) Asymmetric Flow Field Flow Fractionation
Approaches to expand the conventional toolbox for discovery and selection of antibodies with drug-like physicochemical properties
Published in mAbs, 2023
Hristo L. Svilenov, Paolo Arosio, Tim Menzen, Peter Tessier, Pietro Sormanni
Another approach with similar advantages has been developed based on asymmetrical flow field-flow fractionation (AF4), a powerful separation technique, in which the samples are injected and focused onto a membrane in a separation channel.97 The membrane is permeable for the buffer components but not for the analyzed biomolecules. Subsequently, the analytes are eluted from the channel under a cross-flow to enable separation based on diffusion coefficients. The focusing step during AF4 increases the concentration of the analytes close to the membrane, thereby, accentuating protein–protein and protein–membrane interactions that affect the elution profile of the analytes.98