Publications by authors named "Katja Henzler"

This paper presents an X-ray compatible microfluidic platform for characterization of chemical reactions at synchrotron light sources. We demonstrate easy to implement techniques to probe reacting solutions as they first come into contact, and study the very first milliseconds of their reaction in real-time through X-ray absorption spectroscopy (XAS). The devices use polydimethylsiloxane (PDMS) microfluidic channels sandwiched between ultrathin, X-ray transparent silicon nitride observation windows and rigid substrates.

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In viscous, organic-rich aerosol particles containing iron, sunlight may induce anoxic conditions that stabilize reactive oxygen species (ROS) and carbon-centered radicals (CCRs). In laboratory experiments, we show mass loss, iron oxidation and radical formation and release from photoactive organic particles containing iron. Our results reveal a range of temperature and relative humidity, including ambient conditions, that control ROS build up and CCR persistence in photochemically active, viscous organic particles.

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Mechanisms of CaCO nucleation from solutions that depend on multistage pathways and the existence of species far more complex than simple ions or ion pairs have recently been proposed. Herein, we provide a tightly coupled theoretical and experimental study on the pathways that precede the initial stages of CaCO nucleation. Starting from molecular simulations, we succeed in correctly predicting bulk thermodynamic quantities and experimental data, including equilibrium constants, titration curves, and detailed x-ray absorption spectra taken from the supersaturated CaCO solutions.

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The immobilization of bovine serum albumins (BSA) onto cationic spherical polyelectrolyte brushes (SPB) consisting of a solid polystyrene (PS) core and a densely grafted poly(2-aminoethyl methacrylate hydrochloride) (PAEMH) shell was studied by small-angle X-ray scattering (SAXS). The observed dynamics of adsorption of BSA onto SPB by time-resolved SAXS can be divided into two stages. In the first stage (tens of milliseconds), the added proteins as in-between bridge instantaneously caused the aggregation of SPB.

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Mast cells play an important role in allergic responses. During activation, these cells undergo degranulation, a process by which various kinds of mediators stored in the granules are released. Granule homeostasis in mast cells has mainly been studied by electron microscopy (EM), where the fine structures of subcellular organelles are partially destroyed during sample preparation.

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Background: Recent advances in nanoparticle design have generated new possibilities for nano-biotechnology and nano-medicine. Here we used cryo-soft X-ray tomography (cryo-SXT) to collect comprehensive three-dimensional (3D) data to characterise the interaction of superparamagnetic iron oxide nanoparticles (SPION) with a breast cancer cell line.

Results: We incubated MCF-7 (a human breast cancer cell line) from 0 to 24 h with SPION (15 nm average diameter, coated with dimercaptosuccinic acid), a system that has been studied previously using various microscopy and bulk techniques.

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Vesicular nucleo-cytoplasmic transport is becoming recognized as a general cellular mechanism for translocation of large cargoes across the nuclear envelope. Cargo is recruited, enveloped at the inner nuclear membrane (INM), and delivered by membrane fusion at the outer nuclear membrane. To understand the structural underpinning for this trafficking, we investigated nuclear egress of progeny herpesvirus capsids where capsid envelopment is mediated by two viral proteins, forming the nuclear egress complex (NEC).

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In order to take full advantage of novel functional materials in the next generation of sensorial devices scalable processes for their fabrication and utilization are of great importance. Also understanding the processes lending the properties to those materials is essential. Among the most sought-after sensor applications are low-cost, highly sensitive and selective metal oxide based gas sensors.

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Mesenchymal stromal cells (MSCs) are promising candidates in regenerative cell-therapies. However, optimizing their number and route of delivery remains a critical issue, which can be addressed by monitoring the MSCs' bio-distribution in vivo using super-paramagnetic iron-oxide nanoparticles (SPIONs). In this study, amino-polyvinyl alcohol coated (A-PVA) SPIONs are introduced for cell-labeling and visualization by magnetic resonance imaging (MRI) of human MSCs.

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Correlative fluorescence and soft X-ray cryo-microscopy/tomography on flat sample holders is perfectly suited to study the uncompromised physiological status of adherent cells at its best possible preservation by imaging after fast cryo-immobilization. To understand the mechanism by which herpesviruses induce nucleoplasmic reticulum, i.e.

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Cryo-soft X-ray tomography (cryo-SXT) is a powerful imaging technique that can extract ultrastructural information from whole, unstained mammalian cells as close to the living state as possible. Subcellular organelles including the nucleus, the Golgi apparatus and mitochondria have been identified by morphology alone, due to the similarity in contrast to transmission electron micrographs. In this study, we used cryo-SXT to image endosomes and autophagosomes, organelles that are particularly susceptible to chemical fixation artefacts during sample preparation for electron microscopy.

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The electronic structure of individual hybrid particles was studied by nanoscale near-edge X-ray absorption spectromicroscopy. The colloidal particles consist of a solid polystyrene core and a cross-linked poly-N-(isopropylacrylamide) shell with embedded crystalline titanium dioxide (TiO(2)) nanoparticles (d = 6 ± 3 nm). The TiO(2) particles are generated in the carrier network by a sol-gel process at room temperature.

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We present an investigation of β-lactoglobulin adsorption onto spherical polyelectrolyte brushes (SPBs) by small angle X-ray scattering (SAXS). The SPB consists of a polystyrene core onto which long chains of poly(styrene sulfonate) are grafted. The amount and the distribution of proteins adsorbed in the brush layer at low ionic strength can be derived from SAXS.

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The fabrication of heteroaggregates comprising inorganic and organic nanoparticles of different sizes is reported. Control over the assembly of nanoscale functional building units is of great significance to many practical applications. Joining together different spherical nanoparticles in a defined manner allows control over the shape of the composites.

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The thermodynamics and the driving forces of the adsorption of beta-lactoglobulin on spherical polyelectrolyte brushes (SPB) are investigated by isothermal titration calorimetry (ITC). The SPB consist of a polystyrene core onto which long chains of poly(styrene sulfonate) are grafted. Adsorption isotherms are obtained from measurements by ITC.

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We present the first time-resolved investigation of motions of proteins in densely grafted layers of spherical polyelectrolyte brushes. Using small-angle x-ray scattering combined with rapid stopped-flow mixing, we followed the uptake of bovine serum albumin by poly(acrylic acid) layer with high spatial and temporal resolution. We find that the total amount of adsorbed protein scales with time as t(1/4).

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The activity of adsorbed beta-glucosidase onto spherical polyelectrolyte brushes (SPBs) is investigated by UV-Vis spectroscopy and isothermal titration calorimetry (ITC). By comparing the results of these two methods, we demonstrate that ITC is a precise method for the study of the activity of immobilized enzymes. The carrier particles used for immobilization here consist of a polystyrene core onto which poly(acrylic acid) chains are grafted.

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The adsorption of bovine hemoglobin (BHb) onto colloidal spherical polyelectrolyte brushes (SPBs) is studied by a combination of small-angle X-ray scattering (SAXS) and Fourier transform infrared spectroscopy (FTIR). The SPBs consist of a polystyrene core onto which long chains of poly(styrene sulfonic acid) are grafted. Hemoglobin is a tetrameric protein that disassembles at low pH's and high ionic strengths.

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