@article{SchollMoraisGabrieletal.2017, author = {Scholl, Fabio and Morais, Paulo and Gabriel, Rayla and Sch{\"o}ning, Michael Josef and Siqueira, Jose Roberto, Jr. and Caseli, Luciano}, title = {Carbon nanotubes arranged as smart interfaces in lipid Langmuir-Blodgett films enhancing the enzymatic properties of penicillinase for biosensing applications}, series = {Applied Materials \& Interfaces}, volume = {9}, journal = {Applied Materials \& Interfaces}, number = {36}, publisher = {ACS}, address = {Washington}, issn = {1944-8252}, doi = {10.1021/acsami.7b08095}, pages = {31054 -- 31066}, year = {2017}, abstract = {In this paper, carbon nanotubes (CNTs) were incorporated in penicillinase-phospholipid Langmuir and Langmuir-Blodgett (LB) films to enhance the enzyme catalytic properties. Adsorption of the penicillinase and CNTs at dimyristoylphosphatidic acid (DMPA) monolayers at the air-water interface was investigated by surface pressure-area isotherms, vibrational spectroscopy, and Brewster angle microscopy. The floating monolayers were transferred to solid supports through the LB technique, forming mixed DMPA-CNTs-PEN films, which were investigated by quartz crystal microbalance, vibrational spectroscopy, and atomic force microscopy. Enzyme activity was studied with UV-vis spectroscopy and the feasibility of the supramolecular device nanostructured as ultrathin films were essayed in a capacitive electrolyte-insulator-semiconductor (EIS) sensor device. The presence of CNTs in the enzyme-lipid LB film not only tuned the catalytic activity of penicillinase but also helped conserve its enzyme activity after weeks, showing increased values of activity. Viability as penicillin sensor was demonstrated with capacitance/voltage and constant capacitance measurements, exhibiting regular and distinctive output signals over all concentrations used in this work. These results may be related not only to the nanostructured system provided by the film, but also to the synergism between the compounds on the active layer, leading to a surface morphology that allowed a fast analyte diffusion because of an adequate molecular accommodation, which also preserved the penicillinase activity. This work therefore demonstrates the feasibility of employing LB films composed of lipids, CNTs, and enzymes as EIS devices for biosensing applications.}, language = {en} } @article{TranMottaghyArltKoerferetal.2017, author = {Tran, Linda and Mottaghy, K. and Arlt-K{\"o}rfer, Sabine and Waluga, Christian and Behbahani, Mehdi}, title = {An experimental study of shear-dependent human platelet adhesion and underlying protein-binding mechanisms in a cylindrical Couette system}, series = {Biomedizinische Technik}, volume = {62}, journal = {Biomedizinische Technik}, number = {4}, publisher = {De Gruyter}, address = {Berlin}, issn = {0013-5585}, doi = {10.1515/bmt-2015-0034}, pages = {383 -- 392}, year = {2017}, language = {en} } @incollection{TranTranMatthiesetal.2017, author = {Tran, N. T. and Tran, Thanh Ngoc and Matthies, M. G. and Stavroulakis, G. E. and Staat, Manfred}, title = {Shakedown Analysis Under Stochastic Uncertainty by Chance Constrained Programming}, series = {Advances in Direct Methods for Materials and Structures}, booktitle = {Advances in Direct Methods for Materials and Structures}, publisher = {Springer}, address = {Cham}, isbn = {978-3-319-59810-9}, doi = {10.1007/978-3-319-59810-9_6}, pages = {85 -- 103}, year = {2017}, abstract = {In this paper we propose a stochastic programming method to analyse limit and shakedown of structures under uncertainty condition of strength. Based on the duality theory, the shakedown load multiplier formulated by the kinematic theorem is proved actually to be the dual form of the shakedown load multiplier formulated by static theorem. In this investigation a dual chance constrained programming algorithm is developed to calculate simultaneously both the upper and lower bounds of the plastic collapse limit and the shakedown limit. The edge-based smoothed finite element method (ES-FEM) with three-node linear triangular elements is used for structural analysis.}, language = {en} } @article{HonarvarfardGamellaPoghossianetal.2017, author = {Honarvarfard, Elham and Gamella, Maria and Poghossian, Arshak and Sch{\"o}ning, Michael Josef and Katz, Evgeny}, title = {An enzyme-based reversible Controlled NOT (CNOT) logic gate operating on a semiconductor transducer}, series = {Applied Materials Today}, volume = {9}, journal = {Applied Materials Today}, publisher = {Elsevier}, address = {Amsterdam}, issn = {2352-9407}, doi = {10.1016/j.apmt.2017.08.003}, pages = {266 -- 270}, year = {2017}, abstract = {An enzyme-based biocatalytic system mimicking operation of a logically reversible Controlled NOT (CNOT) gate has been interfaced with semiconductor electronic transducers. Electrolyte-insulator-semiconductor (EIS) structures have been used to transduce chemical changes produced by the enzyme system to an electronically readable capacitive output signal using field-effect features of the EIS device. Two enzymes, urease and esterase, were immobilized on the insulating interface of EIS structure producing local pH changes performing XOR logic operation controlled by various combinations of the input signals represented by urea and ethyl butyrate. Another EIS transducer was functionalized with esterase only, thus performing Identity (ID) logic operation for the ethyl butyrate input. Both semiconductor devices assembled in parallel operated as a logically reversible CNOT gate. The present system, despite its simplicity, demonstrated for the first time logically reversible function of the enzyme system transduced electronically with the semiconductor devices. The biomolecular realization of a CNOT gate interfaced with semiconductors is promising for integration into complex biomolecular networks and future biosensor/biomedical applications.}, language = {en} } @article{RoehlenPilasSchoeningetal.2017, author = {R{\"o}hlen, Desiree and Pilas, Johanna and Sch{\"o}ning, Michael Josef and Selmer, Thorsten}, title = {Development of an amperometric biosensor platform for the combined determination of l-Malic, Fumaric, and l-Aspartic acid}, series = {Applied Biochemistry and Biotechnology}, volume = {183}, journal = {Applied Biochemistry and Biotechnology}, publisher = {Springer}, address = {Berlin}, issn = {1559-0291}, doi = {10.1007/s12010-017-2578-1}, pages = {566 -- 581}, year = {2017}, abstract = {Three amperometric biosensors have been developed for the detection of L-malic acid, fumaric acid, and L -aspartic acid, all based on the combination of a malate-specific dehydrogenase (MDH, EC 1.1.1.37) and diaphorase (DIA, EC 1.8.1.4). The stepwise expansion of the malate platform with the enzymes fumarate hydratase (FH, EC 4.2.1.2) and aspartate ammonia-lyase (ASPA, EC 4.3.1.1) resulted in multi-enzyme reaction cascades and, thus, augmentation of the substrate spectrum of the sensors. Electrochemical measurements were carried out in presence of the cofactor β-nicotinamide adenine dinucleotide (NAD+) and the redox mediator hexacyanoferrate (III) (HCFIII). The amperometric detection is mediated by oxidation of hexacyanoferrate (II) (HCFII) at an applied potential of + 0.3 V vs. Ag/AgCl. For each biosensor, optimum working conditions were defined by adjustment of cofactor concentrations, buffer pH, and immobilization procedure. Under these improved conditions, amperometric responses were linear up to 3.0 mM for L-malate and fumarate, respectively, with a corresponding sensitivity of 0.7 μA mM-1 (L-malate biosensor) and 0.4 μA mM-1 (fumarate biosensor). The L-aspartate detection system displayed a linear range of 1.0-10.0 mM with a sensitivity of 0.09 μA mM-1. The sensor characteristics suggest that the developed platform provides a promising method for the detection and differentiation of the three substrates.}, language = {en} } @article{PilasYaziciSelmeretal.2017, author = {Pilas, Johanna and Yazici, Yasemen and Selmer, Thorsten and Keusgen, Michael and Sch{\"o}ning, Michael Josef}, title = {Optimization of an amperometric biosensor array for simultaneous measurement of ethanol, formate, d- and l-lactate}, series = {Electrochimica Acta}, volume = {251}, journal = {Electrochimica Acta}, publisher = {Elsevier}, address = {Amsterdam}, issn = {0013-4686}, doi = {10.1016/j.electacta.2017.07.119}, pages = {256 -- 262}, year = {2017}, abstract = {The immobilization of NAD+-dependent dehydrogenases, in combination with a diaphorase, enables the facile development of multiparametric sensing devices. In this work, an amperometric biosensor array for simultaneous determination of ethanol, formate, d- and l-lactate is presented. Enzyme immobilization on platinum thin-film electrodes was realized by chemical cross-linking with glutaraldehyde. The optimization of the sensor performance was investigated with regard to enzyme loading, glutaraldehyde concentration, pH, cofactor concentration and temperature. Under optimal working conditions (potassium phosphate buffer with pH 7.5, 2.5 mmol L-1 NAD+, 2.0 mmol L-1 ferricyanide, 25 °C and 0.4\% glutaraldehyde) the linear working range and sensitivity of the four sensor elements was improved. Simultaneous and cross-talk free measurements of four different metabolic parameters were performed successfully. The reliable analytical performance of the biosensor array was demonstrated by application in a clarified sample of inoculum sludge. Thereby, a promising approach for on-site monitoring of fermentation processes is provided.}, language = {en} } @article{AlbannaLuekeSjapicetal.2017, author = {Albanna, Walid and Lueke, Jan Niklas and Sjapic, Volha and Kotliar, Konstantin and Hescheler, J{\"u}rgen and Clusmann, Hans and Sjapic, Sergej and Alpdogan, Serdan and Schneider, Toni and Schubert, Gerrit Alexander and Neumaier, Felix}, title = {Electroretinographic Assessment of Inner Retinal Signaling in the Isolated and Superfused Murine Retina}, series = {Current Eye Research}, journal = {Current Eye Research}, number = {Article in press}, publisher = {Taylor \& Francis}, address = {London}, issn = {1460-2202}, doi = {10.1080/02713683.2017.1339807}, pages = {1 -- 9}, year = {2017}, language = {en} } @article{SeifarthGrosseGrossmannetal.2017, author = {Seifarth, Volker and Grosse, Joachim O. and Grossmann, Matthias and Janke, Heinz Peter and Arndt, Patrick and Koch, Sabine and Epple, Matthias and Artmann, Gerhard and Temiz Artmann, Ayseg{\"u}l}, title = {Mechanical induction of bi-directional orientation of primary porcine bladder smooth muscle cells in tubular fibrin-poly(vinylidene fluoride) scaffolds for ureteral and urethral repair using cyclic and focal balloon catheter stimulation}, series = {Journal of Biomaterials Applications}, volume = {32}, journal = {Journal of Biomaterials Applications}, number = {3}, publisher = {Sage}, address = {London}, issn = {1530-8022}, doi = {10.1177/0885328217723178}, pages = {321 -- 330}, year = {2017}, language = {en} } @inproceedings{BreuerGuthmannSchoeningetal.2017, author = {Breuer, Lars and Guthmann, Eric and Sch{\"o}ning, Michael Josef and Thoelen, Ronald and Wagner, Torsten}, title = {Light-Stimulated Hydrogels with Incorporated Graphene Oxide as Actuator Material for Flow Control in Microfluidic Applications}, series = {Proceedings Eurosensors 2017 Conference, Paris, France, 3-6 September 2017}, booktitle = {Proceedings Eurosensors 2017 Conference, Paris, France, 3-6 September 2017}, doi = {10.3390/proceedings1040524}, pages = {1 -- 4}, year = {2017}, language = {en} } @article{Hoettges2017, author = {H{\"o}ttges, J{\"o}rg}, title = {QKan - Management of drainage system data with QGIS}, series = {Free and Open Source Software for Geospatial (FOSS4G) Conference Proceedings}, volume = {17}, journal = {Free and Open Source Software for Geospatial (FOSS4G) Conference Proceedings}, number = {Article 13}, pages = {95 -- 100}, year = {2017}, language = {en} }