@article{MuschallikMolinnusBongaertsetal.2017, author = {Muschallik, Lukas and Molinnus, Denise and Bongaerts, Johannes and Pohl, Martina and Wagner, Torsten and Sch{\"o}ning, Michael Josef and Siegert, Petra and Selmer, Thorsten}, title = {(R,R)-Butane-2,3-diol Dehydrogenase from Bacillus clausii DSM 8716T: Cloning and Expression of the bdhA-Gene, and Initial Characterization of Enzyme}, series = {Journal of Biotechnology}, volume = {258}, journal = {Journal of Biotechnology}, publisher = {Elsevier}, address = {Amsterdam}, issn = {0168-1656}, doi = {10.1016/j.jbiotec.2017.07.020}, pages = {41 -- 50}, year = {2017}, abstract = {The gene encoding a putative (R,R)-butane-2,3-diol dehydrogenase (bdhA) from Bacillus clausii DSM 8716T was isolated, sequenced and expressed in Escherichia coli. The amino acid sequence of the encoded protein is only distantly related to previously studied enzymes (identity 33-43\%) and exhibited some uncharted peculiarities. An N-terminally StrepII-tagged enzyme variant was purified and initially characterized. The isolated enzyme catalyzed the (R)-specific oxidation of (R,R)- and meso-butane-2,3-diol to (R)- and (S)-acetoin with specific activities of 12 U/mg and 23 U/mg, respectively. Likewise, racemic acetoin was reduced with a specific activity of up to 115 U/mg yielding a mixture of (R,R)- and meso-butane-2,3-diol, while the enzyme reduced butane-2,3-dione (Vmax 74 U/mg) solely to (R,R)-butane-2,3-diol via (R)-acetoin. For these reactions only activity with the co-substrates NADH/NAD+ was observed. The enzyme accepted a selection of vicinal diketones, α-hydroxy ketones and vicinal diols as alternative substrates. Although the physiological function of the enzyme in B. clausii remains elusive, the data presented herein clearly demonstrates that the encoded enzyme is a genuine (R,R)-butane-2,3-diol dehydrogenase with potential for applications in biocatalysis and sensor development.}, language = {en} } @article{MiyamotoHayashiSakamotoetal.2017, author = {Miyamoto, Ko-ichiro and Hayashi, Kosuke and Sakamoto, Azuma and Werner, Frederik and Wagner, Torsten and Sch{\"o}ning, Michael Josef and Yoshinobu, Tatsuo}, title = {A high-Q resonance-mode measurement of EIS capacitive sensor by elimination of series resistance}, series = {Sensor and Actuators B: Chemical}, volume = {248}, journal = {Sensor and Actuators B: Chemical}, publisher = {Elsevier}, address = {Amsterdam}, issn = {0925-4005}, doi = {10.1016/j.snb.2017.03.002}, pages = {1006 -- 1010}, year = {2017}, abstract = {An EIS capacitive sensor is a semiconductor-based potentiometric sensor, which is sensitive to the ion concentration or pH value of the solution in contact with the sensing surface. To detect a small change in the ion concentration or pH, a small capacitance change must be detected. Recently, a resonance-mode measurement was proposed, in which an inductor was connected to the EIS capacitive sensor and the resonant frequency was correlated with the pH value. In this study, the Q factor of the resonant circuit was enhanced by canceling the internal resistance of the reference electrode and the internal resistance of the inductor coil with the help of a bypass capacitor and a negative impedance converter, respectively. 1\% variation of the signal in the developed system corresponded to a pH change of 3.93 mpH, which was about 1/12 of the conventional method, suggesting a better performance in detection of a small pH change.}, language = {en} } @article{GaribaldiBegingCaneseetal.2017, author = {Garibaldi, F. and Beging, Stefan and Canese, R. and Carpinelli, G. and Clinthorne, N. and Colilli, S. and Cosentino, L. and Finocchiaro, P. and Giuliani, F. and Gricia, M. and Lucentini, M. and Majewski, S. and Monno, E. and Musico, P. and Santavenere, F. and T{\"o}dter, J. and Wegener, Hans-Peter and Ziemons, Karl}, title = {A novel TOF-PET MRI detector for diagnosis and follow up of the prostate cancer}, series = {European Physical Journal Plus}, volume = {132}, journal = {European Physical Journal Plus}, number = {9}, publisher = {Springer}, address = {Berlin}, issn = {2190-5444}, doi = {10.1140/epjp/i2017-11662-x}, year = {2017}, language = {en} } @article{MuellerJungAhammer2017, author = {M{\"u}ller, Wolfram and Jung, Alexander and Ahammer, Helmut}, title = {Advantages and problems of nonlinear methods applied to analyze physiological time signals: human balance control as an example}, series = {Scientific Reports}, volume = {7}, journal = {Scientific Reports}, number = {Article number 2464}, publisher = {Springer Nature}, address = {Cham}, isbn = {2045-2322}, doi = {10.1038/s41598-017-02665-5}, pages = {1 -- 11}, year = {2017}, language = {en} } @article{EngelmannBuhlBaumannetal.2017, author = {Engelmann, Ulrich M. and Buhl, Eva Miriam and Baumann, Martin and Schmitz-Rode, Thomas and Slabu, Ioana}, title = {Agglomeration of magnetic nanoparticles and its effects on magnetic hyperthermia}, series = {Current Directions in Biomedical Engineering}, volume = {3}, journal = {Current Directions in Biomedical Engineering}, number = {2}, publisher = {De Gruyter}, address = {Berlin}, issn = {2364-5504}, doi = {10.1515/cdbme-2017-0096}, pages = {457 -- 460}, year = {2017}, language = {en} } @article{KotliarHauserOrtneretal.2017, author = {Kotliar, Konstantin and Hauser, Christine and Ortner, Marion and Muggenthaler, Claudia and Diehl-Schmid, Janine and Angermann, Susanne and Hapfelmeier, Alexander and Schmaderer, Christoph and Grimmer, Timo}, title = {Altered neurovascular coupling as measured by optical imaging: a biomarker for Alzheimer's disease}, series = {Scientific Reports}, volume = {7}, journal = {Scientific Reports}, number = {1}, publisher = {Springer Nature}, address = {Cham}, issn = {2045-2322}, doi = {10.1038/s41598-017-13349-5}, pages = {1 -- 11}, year = {2017}, 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{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} } @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{MolinnusPoghossianKeusgenetal.2017, author = {Molinnus, Denise and Poghossian, Arshak and Keusgen, Michael and Katz, Evgeny and Sch{\"o}ning, Michael Josef}, title = {Coupling of Biomolecular Logic Gates with Electronic Transducers: From Single Enzyme Logic Gates to Sense/Act/Treat Chips}, series = {Electroanalysis}, volume = {29}, journal = {Electroanalysis}, number = {8}, publisher = {Wiley}, address = {Weinheim}, issn = {1521-4109}, doi = {10.1002/elan.201700208}, pages = {1840 -- 1849}, year = {2017}, abstract = {The integration of biomolecular logic principles with electronic transducers allows designing novel digital biosensors with direct electrical output, logically triggered drug-release, and closed-loop sense/act/treat systems. This opens new opportunities for advanced personalized medicine in the context of theranostics. In the present work, we will discuss selected examples of recent developments in the field of interfacing enzyme logic gates with electrodes and semiconductor field-effect devices. Special attention is given to an enzyme OR/Reset logic gate based on a capacitive field-effect electrolyte-insulator-semiconductor sensor modified with a multi-enzyme membrane. Further examples are a digital adrenaline biosensor based on an AND logic gate with binary YES/NO output and an integrated closed-loop sense/act/treat system comprising an amperometric glucose sensor, a hydrogel actuator, and an insulin (drug) sensor.}, language = {en} }