| 1. |
- McGinn, Steven, et al.
(author)
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New Technologies for DNA analysis-A review of the READNA Project.
- 2016
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In: New Biotechnology. - : Elsevier BV. - 1876-4347 .- 1871-6784.
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Research review (peer-reviewed)abstract
- The REvolutionary Approaches and Devices for Nucleic Acid analysis (READNA) project received funding from the European Commission for 4 1/2 years. The objectives of the project revolved around technological developments in nucleic acid analysis. The project partners have discovered, created and developed a huge body of insights into nucleic acid analysis, ranging from improvements and implementation of current technologies to the most promising sequencing technologies that constitute a 3(rd) and 4(th) generation of sequencing methods with nanopores and in situ sequencing, respectively.
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| 2. |
- Odelli, Davide, et al.
(author)
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Interaction between Fish Skin Gelatin and Pea Protein at Air-Water Interface after Ultrasound Treatment
- 2022
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In: Foods. - : MDPI AG. - 2304-8158. ; 11:5
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Journal article (peer-reviewed)abstract
- The interaction between fish skin gelatin (FG) and pea protein isolate (PPI) was investigated at the air-water interface (A-W) before and after a high intensity (275 W, 5 min) ultrasound treatment (US). We analyzed the properties of the single protein suspensions as well as an equal ratio of FG:PPI (MIX), in terms of ζ-potential, particle size, molecular weight, bulk viscosity and interfacial tension. The foaming properties were then evaluated by visual analysis and by Turbiscan Tower. Confocal laser scanning microscopy (CLSM) was employed to explore the role of the proteins on the microstructure of foams. The results showed that the ultrasound treatment slightly influenced physicochemical properties of the proteins, while in general, did not significantly affect their behavior both in bulk and at the air-water interface. In particular, PPI aggregate size was reduced (−48 nm) while their negative charges were increased (−1 mV) after the treatment. However, when the proteins were combined, higher molecular weight of aggregates, higher foam stability values (+14%) and lower interfacial tension (IFT) values (47.2 ± 0.2 mN/m) were obtained, leading us to assume that a weak interaction was developed between them.
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| 3. |
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| 4. |
- Marie, Rodolphe, et al.
(author)
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A generic surface modification strategy for sensing applications based on Au/SiO2 nanostructures
- 2007
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In: Biointerphases. - : American Vacuum Society. - 1934-8630 .- 1559-4106. ; 2:1, s. 49-55
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Journal article (peer-reviewed)abstract
- A generic protocol for the creation of material-mediated self-assembled patterns of streptavidin, defined solely by patterns of gold and SiO2, is presented. Protein-adsorption resistance of selected regions was obtained by material-specific adsorption of thiol-modified poly(ethylene)glycol (thiol-PEG) on gold followed by adsorption of poly-L-lysine (PLL) modified PEG (PLL-g-PEG) on SiO2. Selective streptavidin binding to either gold or SiO2 (or both) was ensured by introducing biotin-modified thiolated (thiol-biotin) and/or biotin-modified PLL-g-PEG (PLL-g-PEGbiotin) compounds. The introduction of biotin did not influence the protein-adsorption resistance. On the macroscopic scale, the protein-adsorption-resistant properties and the streptavidin-binding capacity were optimized using quartz crystal microbalance with dissipation monitoring. The reproduction of micrometer-scale gold patterns on SiO2 into patterns of streptavidin was verified using fluorescence microscopy, while the compatibility of the material-specific surface-modification strategy with nanoscale features was accomplished by modifying a localized surface plasmon resonance (LSPR) active template, defined by randomly distributed nanoapertures in a thin gold film on SiO2. The demonstrated compatibility of the latter substrate with LSPR-based label-free sensing of biorecognition reactions, combined with the fact that all compounds utilized are commercially available, makes the surface-modification protocol attractive as a generic surface modification solution for a broad range of biorecognition-based assays. (C) 2007 American Vacuum Society.
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| 6. |
- Marie, Rodolphe, et al.
(author)
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Use of PLL-g-PEG in micro-fluidic devices for localizing selective and specific protein binding
- 2006
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In: Langmuir. - : American Chemical Society (ACS). - 0743-7463 .- 1520-5827. ; 22:24, s. 10103-10108
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Journal article (peer-reviewed)abstract
- By utilizing flow-controlled PLL-g-PEG and PLL-g-PEGbiotin modification of predefined regions of a poly-(dimethylsiloxane) (PDMS) micro-fluidic device, with an intentionally chosen large (similar to 1 cm(2)) internal surface area, we report rapid (10 min), highly localized (6 x 10(-6) cm(2)), and specific surface-based protein capture from a sample volume (100 mu L) containing a low amount of protein (160 attomol in pure buffer and 400 attomol in serum). The design criteria for this surface modification were achieved using QCM-D (quartz crystal microbalance with energy dissipation monitoring) of serum protein adsorption onto PLL-g-PEG-modified oxidized PDMS. Equally good, or almost as good, results were obtained for oxidized SU-8, Topas, and poly(methyl metacrylate) (PMMA), demonstrating the generic potential of PLL-g-PEG for surface modification in various micro-fluidic applications.
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