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  • 101.
    Wells, Daniel J.
    et al.
    La Trobe Univ, Sch Comp Engn & Math Sci, La Trobe Inst Mol Sci, Dept Math & Phys Sci, Bundoora, Vic 3086, Australia..
    Dahlqvist, Caroline
    KTH Royal Inst Technol, AlbaNova Univ Ctr, Dept Appl Phys, Biomed & Xray Phys, SE-10691 Stockholm, Sweden..
    Jonsson, Olof
    KTH Royal Inst Technol, AlbaNova Univ Ctr, Dept Appl Phys, Biomed & Xray Phys, SE-10691 Stockholm, Sweden..
    Sellberg, Jonas A.
    KTH, School of Engineering Sciences (SCI), Applied Physics, Biomedical and X-ray Physics.
    Abbey, Brian
    La Trobe Univ, Sch Comp Engn & Math Sci, La Trobe Inst Mol Sci, Dept Math & Phys Sci, Bundoora, Vic 3086, Australia..
    Martin, Andrew, V
    RMIT Univ, Sch Sci, Melbourne, Vic 3000, Australia..
    Darmanin, Connie
    La Trobe Univ, Sch Comp Engn & Math Sci, La Trobe Inst Mol Sci, Dept Math & Phys Sci, Bundoora, Vic 3086, Australia..
    et al.,
    Observations of phase changes in monoolein during high viscous injection2022In: Journal of Synchrotron Radiation, ISSN 0909-0495, E-ISSN 1600-5775, Vol. 29, no 3, p. 602-614Article in journal (Refereed)
    Abstract [en]

    Serial crystallography of membrane proteins often employs high-viscosity injectors (HVIs) to deliver micrometre-sized crystals to the X-ray beam. Typically, the carrier medium is a lipidic cubic phase (LCP) media, which can also be used to nucleate and grow the crystals. However, despite the fact that the LCP is widely used with HVIs, the potential impact of the injection process on the LCP structure has not been reported and hence is not yet well understood. The self-assembled structure of the LCP can be affected by pressure, dehydration and temperature changes, all of which occur during continuous flow injection. These changes to the LCP structure may in turn impact the results of X-ray diffraction measurements from membrane protein crystals. To investigate the influence of HVIs on the structure of the LCP we conducted a study of the phase changes in monoolein/water and monoolein/buffer mixtures during continuous flow injection, at both atmospheric pressure and under vacuum. The reservoir pressure in the HVI was tracked to determine if there is any correlation with the phase behaviour of the LCP. The results indicated that, even though the reservoir pressure underwent (at times) significant variation, this did not appear to correlate with observed phase changes in the sample stream or correspond to shifts in the LCP lattice parameter. During vacuum injection, there was a three-way coexistence of the gyroid cubic phase, diamond cubic phase and lamellar phase. During injection at atmospheric pressure, the coexistence of a cubic phase and lamellar phase in the monoolein/water mixtures was also observed. The degree to which the lamellar phase is formed was found to be strongly dependent on the co-flowing gas conditions used to stabilize the LCP stream. A combination of laboratory-based optical polarization microscopy and simulation studies was used to investigate these observations.

  • 102.
    Wurm, Christian A.
    et al.
    Max Planck Inst Biophys Chem, Dept NanoBiophoton, Gottingen, Germany.;Abberior Instruments GmbH, Gottingen, Germany..
    Schwarz, Heinz
    Max Planck Inst Dev Biol, Tubingen, Germany..
    Jans, Daniel C.
    KTH, School of Engineering Sciences (SCI), Applied Physics. KTH, Centres, Science for Life Laboratory, SciLifeLab. Max Planck Inst Biophys Chem, Dept NanoBiophoton, Gottingen, Germany.;Univ Med Ctr Gottingen, Clin Neurol, Gottingen, Germany.
    Riedel, Dietmar
    Max Planck Inst Biophys Chem, Lab Electron Microscopy, D-37077 Gottingen, Germany..
    Humbel, Bruno M.
    Univ Lausanne, Electron Microscopy Facil, Lausanne, Switzerland.;Okinawa Inst Sci & Technol, Imaging, Onna Son, Okinawa, Japan..
    Jakobs, Stefan
    Max Planck Inst Biophys Chem, Dept NanoBiophoton, Gottingen, Germany.;Univ Med Ctr Gottingen, Clin Neurol, Gottingen, Germany..
    Correlative STED super-resolution light and electron microscopy on resin sections2019In: Journal of Physics D: Applied Physics, ISSN 0022-3727, E-ISSN 1361-6463, Vol. 52, no 37, article id 374003Article in journal (Refereed)
    Abstract [en]

    Correlative light and electron microscopy approaches can reveal the localisation of specific proteins while providing detailed information on the cellular context, thereby combining the strengths of both imaging modalities. The major challenge in combining fluorescence microscopy with electron microscopy is the different sample preparation requirements necessary for obtaining high quality data from both modalities. To overcome this limitation, we combined conventional sample preparation protocols for electron microscopy with post-embedding labelling on ultra-thin sections using antibodies and other specific ligands. We successfully employed STED super-resolution microscopy to image the subcellular distribution of several targets in various specimen including E. coli, T brucei, S. cerevisiae, human cancer cells and bovine sperm. Thus, we present widely applicable methods facilitating the use of antibodies for correlative super-resolution light and electron microscopy of post-embedding labelled targets.

  • 103.
    Wärnheim, Alexander
    et al.
    KTH. RISE Biosci & Mat, Stockholm, Sweden..
    Toprak, Muhammet
    KTH, School of Industrial Engineering and Management (ITM), Materials Science and Engineering.
    Ahniyaz, Anwar
    RISE Biosci & Mat, Stockholm, Sweden..
    Swerin, Agne
    KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Chemistry, Surface and Corrosion Science. RISE Biosci & Mat, Stockholm, Sweden..
    Abitbol, Tiffany
    RISE Bioecon, Stockholm, Sweden..
    Nanocellulose-based hybrid materials for optical applications2019In: Abstracts of Papers of the American Chemical Society, ISSN 0065-7727, Vol. 257Article in journal (Other academic)
  • 104.
    Xie, Li
    et al.
    KTH, School of Information and Communication Technology (ICT), Electronic Systems. KTH, School of Information and Communication Technology (ICT), Centres, VinnExcellence Center for Intelligence in Paper and Packaging, iPACK.
    Yang, Geng
    KTH, School of Information and Communication Technology (ICT), Electronic Systems. KTH, School of Information and Communication Technology (ICT), Centres, VinnExcellence Center for Intelligence in Paper and Packaging, iPACK.
    Mantysalo, Matti
    TUT.
    Jonsson, Fredrik
    KTH, School of Information and Communication Technology (ICT), Electronic Systems. KTH, School of Information and Communication Technology (ICT), Centres, VinnExcellence Center for Intelligence in Paper and Packaging, iPACK.
    Zheng, Li-Rong
    KTH, School of Information and Communication Technology (ICT), Electronic Systems. KTH, School of Information and Communication Technology (ICT), Centres, VinnExcellence Center for Intelligence in Paper and Packaging, iPACK.
    A system-on-chip and paper-based inkjet printed electrodes for a hybrid wearable bio-sensing system2012In: Engineering in Medicine and Biology Society (EMBC), 2012 Annual International Conference of the IEEE, IEEE , 2012, p. 5026-5029Conference paper (Refereed)
    Abstract [en]

    This paper presents a hybrid wearable bio-sensing system, which combines traditional small-area low-power and high-performance System-on-Chip (SoC), flexible paper substrate and cost-effective Printed Electronics. Differential bio-signals are measured, digitized, stored and transmitted by the SoC. The total area of the chip is 1.5 × 3.0 mm2. This enables the miniaturization of the wearable system. The electrodes and interconnects are inkjet printed on paper substrate and the performance is verified in in-vivo tests. The quality of electrocardiogram signal sensed by printed electrodes is comparable with commercial electrodes, with noise level slightly increased. The paper-based inkjet printed system is flexible, light and thin, which makes the final system comfortable for end-users. The hybrid bio-sensing system offers a potential solution to the next generation wearable healthcare technology.

  • 105. Yassin, M. A.
    et al.
    Leknes, K. N.
    Sun, Yang
    KTH, School of Chemical Science and Engineering (CHE), Fibre and Polymer Technology.
    Lie, S. A.
    Finne-Wistrand, Anna
    KTH, School of Chemical Science and Engineering (CHE), Fibre and Polymer Technology.
    Mustafa, K.
    Surfactant tuning of hydrophilicity of porous degradable copolymer scaffolds promotes cellular proliferation and enhances bone formation2016In: Journal of Biomedical Materials Research. Part A, ISSN 1549-3296, E-ISSN 1552-4965Article in journal (Refereed)
    Abstract [en]

    Poly(l-lactide-co-e(open)-caprolactone) (poly(LLA-co-CL)) has been blended with Tween 80 to tune the material properties and optimize cell-material interactions. Accordingly, the aims of this study were fourfold: to evaluate the effect of low concentrations of Tween 80 on the surface microstructure of 3D poly(LLA-co-CL) porous scaffolds: to determine the effect of different concentrations of Tween 80 on proliferation of bone marrow stromal cells (BMSCs) in vitro under dynamic cell culture at 7 and 21 days; to assess the influence of Tween 80 on the degradation rate of poly(LLA-co-CL) at 7 and 21 days; and in a subcutaneous rat model, to evaluate the effect on bone formation of porous scaffolds modified with 3% Tween 80 at 2 and 8 weeks. Blending 3% (w/w) Tween 80 with poly(LLA-co-CL) improves the surface wettability (p<0.001). Poly(LLA-co-CL)/3% Tween 80 shows significantly increased cellular proliferation at days 7 and 21 (p<0.001). Moreover, the presence of Tween 80 facilitates the degradation of poly(LLA-co-CL). Two weeks post-implantation, the poly(LLA-co-CL)/3% Tween 80 scaffolds exhibit significant mRNA expression of Runx2 (p=0.004). After 8 weeks, poly(LLA-co-CL)/3% Tween 80 scaffolds show significantly increased de novo bone formation, demonstrated by μ-CT (p=0.0133) and confirmed histologically. It can be concluded that blending 3% (w/w) Tween 80 with poly (LLA-co-CL) improves the hydrophilicity and osteogenic potential of the scaffolds.

  • 106.
    Zheng, W.
    et al.
    Department of Laboratory Medicine, Karolinska Institute, Huddinge, 141 86, Sweden.
    Boada, R.
    Centre GTS, Department of Chemistry, Autonomous University of Barcelona, Barcelona, 08193, Spain.
    He, R.
    Department of Laboratory Medicine, Karolinska Institute, Huddinge, 141 86, Sweden.
    Xiao, T.
    Centre GTS, Department of Chemistry, Autonomous University of Barcelona, Barcelona, 08193, Spain.
    Fei, Ye
    KTH, School of Engineering Sciences (SCI), Applied Physics, Materials and Nanophysics.
    Simonelli, L.
    CELLS-ALBA Synchrotron Radiation Facility, Carrer de la Llum 2-26, Barcelona, 08290, Spain.
    Valiente, M.
    Centre GTS, Department of Chemistry, Autonomous University of Barcelona, Barcelona, 08193, Spain.
    Zhao, Y.
    Department of Laboratory Medicine, Karolinska Institute, Huddinge, 141 86, Sweden. ECM, Clinical Research Center, Karolinska University Hospital, Huddinge, 141 86, Sweden.
    Hassan, M.
    Department of Laboratory Medicine, Karolinska Institute, Huddinge, 141 86, Sweden. ECM, Clinical Research Center, Karolinska University Hospital, Huddinge, 141 86, Sweden.
    Extracellular albumin covalently sequesters selenocompounds and determines cytotoxicity2019In: International Journal of Molecular Sciences, ISSN 1661-6596, E-ISSN 1422-0067, Vol. 20, no 19, article id 4734Article in journal (Refereed)
    Abstract [en]

    Selenocompounds (SeCs) are well-known nutrients and promising candidates for cancer therapy; however, treatment efficacy is very heterogeneous and the mechanism of action is not fully understood. Several SeCs have been reported to have albumin-binding ability, which is an important factor in determining the treatment efficacy of drugs. In the present investigation, we hypothesized that extracellular albumin might orchestrate SeCs efficacy. Four SeCs representing distinct categories were selected to investigate their cytotoxicity, cellular uptake, and species transformation. Concomitant treatment of albumin greatly decreased cytotoxicity and cellular uptake of SeCs. Using both X-ray absorption spectroscopy and hyphenated mass spectrometry, we confirmed the formation of macromolecular conjugates between SeCs and albumin. Although the conjugate was still internalized, possibly via albumin scavenger receptors expressed on the cell surface, the uptake was strongly inhibited by excess albumin. In summary, the present investigation established the importance of extracellular albumin binding in determining SeCs cytotoxicity. Due to the fact that albumin content is higher in humans and animals than in cell cultures, and varies among many patient categories, our results are believed to have high translational impact and clinical implications.

123 101 - 106 of 106
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