Danube University Krems

About: Danube University Krems is a education organization based out in Krems, Niederösterreich, Austria. It is known for research contribution in the topics: Stroke & Population. The organization has 498 authors who have published 1572 publications receiving 68797 citations.

Novel high resolution MOEMS inclination sensor

Abstract: Inclination sensors are essential elements in many different fields of application such as navigation, metrology, geodetics, geoscience, as well as in the consumer market. In general, for high precision navigation. The sensor's resolution is one of the key parameters to improve the performance and to open up new areas of applications. The implementation of a miniaturized optical readout is one of the most promising ways to accomplish this goal. This paper discusses the principle of a novel inclination sensor along with obtained measurements of two prototypes with different mechanical parameters. The achieved sensitivity is 0.044 V/° resulting in an angular resolution of 0.0051°.

Adsorption of the inflammatory mediator high-mobility group box 1 by polymers with different charge and porosity.

Abstract: High-mobility group box 1 protein (HMGB1) is a conserved protein with a variety of biological functions inside as well as outside the cell. When released by activated immune cells, it acts as a proinflammatory cytokine. Its delayed release has sparked the interest in HMGB1 as a potential therapeutic target. Here, we studied the adsorption of HMGB1 to anionic methacrylate-based polymers as well as to neutral polystyrene-divinylbenzene copolymers. Both groups of adsorbents exhibited efficient binding of recombinant HMGB1 and of HMGB1 derived from lipopolysaccharide-stimulated peripheral blood mononuclear cells. The adsorption characteristics depended on particle size, porosity, accessibility of the pores, and charge of the polymers. In addition to these physicochemical parameters of the adsorbents, modifications of the molecule itself (e.g., acetylation, phosphorylation, and oxidation), interaction with other plasma proteins or anticoagulants (e.g., heparin), or association with extracellular microvesicles may influence the binding of HMGB1 to adsorbents and lead to preferential depletion of HMGB1 subsets with different biological activity.

Cooperation and Quality Assurance in Technical Translation Projects

Abstract: The professional profile emerging to address today’s demands in business and industry bears little resemblance to the traditional view of translators as solitary all-rounders. Translators and technical writers are now increasingly seen as problem-solvers, working in teams and interacting with other experts. They act as text coordinators, language leads, localisers, information designers or content managers.

Blood Compatibility-An Important but Often Forgotten Aspect of the Characterization of Antimicrobial Peptides for Clinical Application.

Abstract: Acylation of antimicrobial peptides mimics the structure of the natural lipopeptide polymyxin B, and increases antimicrobial and endotoxin-neutralizing activities. In this study, the antimicrobial properties of lactoferrin-based LF11 peptides as well as blood compatibility as a function of acyl chain length were investigated. Beyond the classical hemolysis test, the biocompatibility was determined with human leukocytes and platelets, and the influence of antimicrobial peptides (AMPs) on the plasmatic coagulation and the complement system was investigated. The results of this study show that the acylation of cationic peptides significantly reduces blood tolerance. With increasing acyl chain length, the cytotoxicity of LF11 peptides to human blood cells also increased. This study also shows that acylated cationic antimicrobial peptides are inactivated by the presence of heparin. In addition, it could be shown that the immobilization of LF11 peptides leads to a loss of their antimicrobial properties.

A Sensitive Voltammetric Biosensor for Escherichia Coli Detection Using an Electroactive Substrate for $\beta$ -D-Glucuronidase

Abstract: In this paper, we developed a sensitive and simple electrochemical method for the rapid detection of Escherichia coli in water samples. The general principle of the assay utilizes the enzyme $\beta $ -D-glucuronidase. This enzyme was induced by adding methyl- $\beta $ -D-glucuronide sodium salt and its activity promoted the cleavage of 8-hydroxyquinoline glucuronide to the electroactive compound 8-hydroxyquinoline. This cleavage product was further oxidized on the working electrode of a potentiostat using cyclic voltammetry. The obtained current output signal in a specific voltage range (400 to 600 mV) indicated enzyme activity and subsequently was an evidence for E. coli cells in the sample. For our experiment, we designed a low-cost potentiostat and show an evaluation of this instrument. First, the $\beta $ -D-glucuronidase assay was tested with various concentrations of enzyme solutions before living E. coli cells were investigated. Our presented method allowed a clear and a sensitive identification of 1 colony-forming unit of E. coli without any interference from other investigated bacterial strains. Comprising only few working steps (filtration, incubation, and voltammetric analysis), the method allowed incorporation into an automated prototype that delivered results similar to those obtained from samples treated in laboratory.