TY - JOUR A1 - Scholl, Fabio A1 - Morais, Paulo A1 - Gabriel, Rayla A1 - Schöning, Michael Josef A1 - Siqueira, Jose Roberto, Jr. A1 - Caseli, Luciano T1 - Carbon nanotubes arranged as smart interfaces in lipid Langmuir-Blodgett films enhancing the enzymatic properties of penicillinase for biosensing applications JF - Applied Materials & Interfaces N2 - 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. Y1 - 2017 U6 - https://doi.org/10.1021/acsami.7b08095 SN - 1944-8252 VL - 9 IS - 36 SP - 31054 EP - 31066 PB - ACS CY - Washington ER - TY - JOUR A1 - Tran, Linda A1 - Mottaghy, K. A1 - Arlt-Körfer, Sabine A1 - Waluga, Christian A1 - Behbahani, Mehdi T1 - An experimental study of shear-dependent human platelet adhesion and underlying protein-binding mechanisms in a cylindrical Couette system JF - Biomedizinische Technik Y1 - 2017 U6 - https://doi.org/10.1515/bmt-2015-0034 SN - 0013-5585 VL - 62 IS - 4 SP - 383 EP - 392 PB - De Gruyter CY - Berlin ER - TY - CHAP A1 - Miyamoto, Ko-ichiro A1 - Suto, Takeyuki A1 - Werner, Frederik A1 - Wagner, Torsten A1 - Schöning, Michael Josef A1 - Yoshinobu, Tatsuo T1 - Restraining the Diffusion of Photocarriers to Improve the Spatial Resolution of the Chemical Imaging Sensor T2 - MDPI Proceedings Y1 - 2017 U6 - https://doi.org/10.3390/proceedings1040477 N1 - Eurosensors 2017 Conference, Paris, France, 3–6 September 2017 VL - 1 IS - 4 ER - TY - CHAP A1 - Oberländer, Jan A1 - Arreola, Julio A1 - Hansen, Christina A1 - Greeff, Anton A1 - Mayer, Marlena A1 - Keusgen, Michael A1 - Schöning, Michael Josef T1 - Impedimetric Biosensor to Enable Fast Evaluation of Gaseous Sterilization Processes T2 - MDPI Proceedings Y1 - 2017 U6 - https://doi.org/10.3390/proceedings1040435 N1 - Eurosensors 2017 Conference, Paris, France, 3–6 September 2017 VL - 1 IS - 4 ER - TY - JOUR A1 - Figueroa-Miranda, Gabriela A1 - Feng, Lingyan A1 - Shiu, Simon Chi-Chin A1 - Dirkzwager, Roderick Marshall A1 - Cheung, Yee-Wai A1 - Tanner, Julian Alexander A1 - Schöning, Michael Josef A1 - Offenhäusser, Andreas A1 - Mayer, Dirk T1 - Aptamer-based electrochemical biosensor for highly sensitive and selective malaria detection with adjustable dynamic response range and reusability JF - Sensor and Actuators B: Chemical N2 - Malaria infection remains a significant risk for much of the population of tropical and subtropical areas, particularly in developing countries. Therefore, it is of high importance to develop sensitive, accurate and inexpensive malaria diagnosis tests. Here, we present a novel aptamer-based electrochemical biosensor (aptasensor) for malaria detection by impedance spectroscopy, through the specific recognition between a highly discriminatory DNA aptamer and its target Plasmodium falciparum lactate dehydrogenase (PfLDH). Interestingly, due to the isoelectric point (pI) of PfLDH, the aptasensor response showed an adjustable detection range based on the different protein net-charge at variable pH environments. The specific aptamer recognition allows sensitive protein detection with an expanded detection range and a low detection limit, as well as a high specificity for PfLDH compared to analogous proteins. The specific feasibility of the aptasensor is further demonstrated by detection of the target PfLDH in human serum. Furthermore, the aptasensor can be easily regenerated and thus applied for multiple usages. The robustness, sensitivity, and reusability of the presented aptasensor make it a promising candidate for point-of-care diagnostic systems. Y1 - 2018 U6 - https://doi.org/10.1016/j.snb.2017.07.117 SN - 0925-4005 VL - 255 IS - P1 SP - 235 EP - 243 PB - Elsevier CY - Amsterdam ER - TY - JOUR A1 - Morais, Paulo V. A1 - Gomes, Vanderley F., Jr. A1 - Silva, Anielle C. A. A1 - Dantas, Noelio O. A1 - Schöning, Michael Josef A1 - Siqueira, José R., Jr. T1 - Nanofilm of ZnO nanocrystals/carbon nanotubes as biocompatible layer for enzymatic biosensors in capacitive field-effect devices JF - Journal of Materials Science N2 - The incorporation of nanomaterials that are biocompatible with different types of biological compounds has allowed the development of a new generation of biosensors applied especially in the biomedical field. In particular, the integration of film-based nanomaterials employed in field-effect devices can be interesting to develop biosensors with enhanced properties. In this paper, we studied the fabrication of sensitive nanofilms combining ZnO nanocrystals and carbon nanotubes (CNTs), prepared by means of the layer-by-layer (LbL) technique, in a capacitive electrolyte-insulator-semiconductor (EIS) structure for detecting glucose and urea. The ZnO nanocrystals were incorporated in a polymeric matrix of poly(allylamine) hydrochloride (PAH), and arranged with multi-walled CNTs in a LbL PAH-ZnO/CNTs film architecture onto EIS chips. The electrochemical characterizations were performed by capacitance–voltage and constant capacitance measurements, while the morphology of the films was characterized by atomic force microscopy. The enzymes glucose oxidase and urease were immobilized on film’s surface for detection of glucose and urea, respectively. In order to obtain glucose and urea biosensors with optimized amount of sensitive films, we investigated the ideal number of bilayers for each detection system. The glucose biosensor showed better sensitivity and output signal for an LbL PAH-ZnO/CNTs nanofilm with 10 bilayers. On the other hand, the urea biosensor presented enhanced properties even for the first bilayer, exhibiting high sensitivity and output signal. The presence of the LbL PAH-ZnO/CNTs films led to biosensors with better sensitivity and enhanced response signal, demonstrating that the adequate use of nanostructured films is feasible for proof-of-concept biosensors with improved properties that may be employed for biomedical applications. Y1 - 2017 U6 - https://doi.org/10.1007/s10853-017-1369-y SN - 1573-4803 VL - 52 IS - 20 SP - 12314 EP - 12325 PB - Springer CY - Berlin ER - TY - JOUR A1 - Röhlen, Desiree A1 - Pilas, Johanna A1 - Schöning, Michael Josef A1 - Selmer, Thorsten T1 - Development of an amperometric biosensor platform for the combined determination of l-Malic, Fumaric, and l-Aspartic acid JF - Applied Biochemistry and Biotechnology N2 - 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. Y1 - 2017 U6 - https://doi.org/10.1007/s12010-017-2578-1 SN - 1559-0291 VL - 183 SP - 566 EP - 581 PB - Springer CY - Berlin ER - TY - JOUR A1 - Pilas, Johanna A1 - Yazici, Yasemen A1 - Selmer, Thorsten A1 - Keusgen, Michael A1 - Schöning, Michael Josef T1 - Optimization of an amperometric biosensor array for simultaneous measurement of ethanol, formate, d- and l-lactate JF - Electrochimica Acta N2 - 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. KW - Simultaneous determination KW - Enzymatic biosensor KW - Diaphorase KW - Dehydrogenase Y1 - 2017 U6 - https://doi.org/10.1016/j.electacta.2017.07.119 SN - 0013-4686 VL - 251 SP - 256 EP - 262 PB - Elsevier CY - Amsterdam ER - TY - JOUR A1 - Albanna, Walid A1 - Lueke, Jan Niklas A1 - Sjapic, Volha A1 - Kotliar, Konstantin A1 - Hescheler, Jürgen A1 - Clusmann, Hans A1 - Sjapic, Sergej A1 - Alpdogan, Serdan A1 - Schneider, Toni A1 - Schubert, Gerrit Alexander A1 - Neumaier, Felix T1 - Electroretinographic Assessment of Inner Retinal Signaling in the Isolated and Superfused Murine Retina JF - Current Eye Research Y1 - 2017 U6 - https://doi.org/10.1080/02713683.2017.1339807 SN - 1460-2202 IS - Article in press SP - 1 EP - 9 PB - Taylor & Francis CY - London ER - TY - CHAP A1 - Breuer, Lars A1 - Guthmann, Eric A1 - Schöning, Michael Josef A1 - Thoelen, Ronald A1 - Wagner, Torsten T1 - Light-Stimulated Hydrogels with Incorporated Graphene Oxide as Actuator Material for Flow Control in Microfluidic Applications T2 - Proceedings Eurosensors 2017 Conference, Paris, France, 3–6 September 2017 Y1 - 2017 U6 - https://doi.org/10.3390/proceedings1040524 SP - 1 EP - 4 ER -