@article{BauerEremenkoEhrentreichFoersteretal.1996, author = {Bauer, Christian G. and Eremenko, A. V. and Ehrentreich-F{\"o}rster, Eva and Bier, Frank Fabian and Makower, Alexander and Halsall, H. B. and Heineman, W. R. and Scheller, Frieder W.}, title = {Zeptomole-detecting biosensor for alkaline phosphatase in an electroche mical immunoassay for 2,4- dichlorophenoacetic acid}, year = {1996}, language = {en} } @article{SchellerSchubertBier1995, author = {Scheller, Frieder W. and Schubert, Florian and Bier, Frank Fabian}, title = {Vom Biosensor zur Nanobiotechnologie}, year = {1995}, language = {de} } @article{WarmtFenzelHenkeletal.2021, author = {Warmt, Christian and Fenzel, Carolin Kornelia and Henkel, J{\"o}rg and Bier, Frank Fabian}, title = {Using Cy5-dUTP labelling of RPA-amplicons with downstream microarray analysis for the detection of antibiotic resistance genes}, series = {Scientific reports}, volume = {11}, journal = {Scientific reports}, number = {1}, publisher = {Macmillan Publishers Limited, part of Springer Nature}, address = {[London]}, issn = {2045-2322}, doi = {10.1038/s41598-021-99774-z}, pages = {9}, year = {2021}, abstract = {In this report we describe Cy5-dUTP labelling of recombinase-polymerase-amplification (RPA) products directly during the amplification process for the first time. Nucleic acid amplification techniques, especially polymerase-chain-reaction as well as various isothermal amplification methods such as RPA, becomes a promising tool in the detection of pathogens and target specific genes. Actually, RPA even provides more advantages. This isothermal method got popular in point of care diagnostics because of its speed and sensitivity but requires pre-labelled primer or probes for a following detection of the amplicons. To overcome this disadvantages, we performed an labelling of RPA-amplicons with Cy5-dUTP without the need of pre-labelled primers. The amplification results of various multiple antibiotic resistance genes indicating great potential as a flexible and promising tool with high specific and sensitive detection capabilities of the target genes. After the determination of an appropriate rate of 1\% Cy5-dUTP and 99\% unlabelled dTTP we were able to detect the bla(CTX-M15) gene in less than 1.6E-03 ng genomic DNA corresponding to approximately 200 cfu of Escherichia coli cells in only 40 min amplification time.}, language = {en} } @article{BierEhrentreichFoersterSchelleretal.1996, author = {Bier, Frank Fabian and Ehrentreich-F{\"o}rster, Eva and Scheller, Frieder W. and Makower, Alexander and Eremenko, A. V. and Wollenberger, Ursula and Bauer, Christian G. and Pfeiffer, Dorothea and Micheel, Burkhard}, title = {Ultrasensitive biosensors}, year = {1996}, language = {en} } @article{SchellerBier2002, author = {Scheller, Frieder W. and Bier, Frank Fabian}, title = {Trends in der Bioanalytik}, year = {2002}, language = {de} } @article{SchmitzHertzbergLieseTerjungetal.2014, author = {Schmitz-Hertzberg, Sebastian-Tim and Liese, Rick and Terjung, Carsten and Bier, Frank Fabian}, title = {Towards a smart encapsulation system for small-sized electronic devices: a new approach}, series = {International journal of polymer science}, journal = {International journal of polymer science}, publisher = {Hindawi Publishing Corp.}, address = {New York}, issn = {1687-9422}, doi = {10.1155/2014/713603}, pages = {12}, year = {2014}, abstract = {Miniaturized analytical chip devices like biosensors nowadays provide assistance in highly diverse fields of application such as point-of-care diagnostics and industrial bioprocess engineering. However, upon contact with fluids, the sensor requires a protective shell for its electrical components that simultaneously offers controlled access for the target analytes to the measuring units. We therefore developed a capsule that comprises a permeable and a sealed compartment consisting of variable polymers such as biocompatible and biodegradable polylactic acid (PLA) for medical applications or more economical polyvinyl chloride (PVC) and polystyrene (PS) polymers for bioengineering applications. Production of the sealed capsule compartments was performed by heat pressing of polymer pellets placed in individually designable molds. Controlled permeability of the opposite compartments was achieved by inclusion of NaCl inside the polymer matrix during heat pressing, followed by its subsequent release in aqueous solution. Correlating diffusion rates through the so made permeable capsule compartments were quantified for preselected model analytes: glucose, peroxidase, and polystyrene beads of three different diameters (1.4 mu m, 4.2 mu m, and 20.0 mu m). In summary, the presented capsule system turned out to provide sufficient shelter for small-sized electronic devices and gives insight into its potential permeability for defined substances of analytical interest.}, language = {en} } @article{SachseWuestenhagenSamalikovaetal.2013, author = {Sachse, Rita and W{\"u}stenhagen, Doreen Anja and Samalikova, Maria and Gerrits, Michael and Bier, Frank Fabian and Kubick, Stefan}, title = {Synthesis of membrane proteins in eukaryotic cell-free systems}, series = {Engineering in life sciences : Industry, Environment, Plant, Food}, volume = {13}, journal = {Engineering in life sciences : Industry, Environment, Plant, Food}, number = {1}, publisher = {Wiley-Blackwell}, address = {Hoboken}, issn = {1618-0240}, doi = {10.1002/elsc.201100235}, pages = {39 -- 48}, year = {2013}, abstract = {Cell-free protein synthesis (CFPS) is a valuable method for the fast expression of difficult-to-express proteins as well as posttranslationally modified proteins. Since cell-free systems circumvent possible cytotoxic effects caused by protein overexpression in living cells, they significantly enlarge the scale and variety of proteins that can be characterized. We demonstrate the high potential of eukaryotic CFPS to express various types of membrane proteins covering a broad range of structurally and functionally diverse proteins. Our eukaryotic cell-free translation systems are capable to provide high molecular weight membrane proteins, fluorescent-labeled membrane proteins, as well as posttranslationally modified proteins for further downstream analysis.}, language = {en} } @article{ReissHoelzelBier2009, author = {Reiss, Edda and Hoelzel, Ralph and Bier, Frank Fabian}, title = {Synthesis and stretching of rolling circle amplification products in a flow-through system}, issn = {1613-6810}, doi = {10.1002/smll.200900319}, year = {2009}, abstract = {Enzymatic isothermal rolling circle amplification (RCA) produces long concatemeric single-stranded DNA (ssDNA) molecules if a small circular ssDNA molecule is applied as the template. A method is presented here in which the RCA reaction is carried out in a flow-through system, starting from isolated surface-tethered DNA primers. This approach combines gentle fluidic handling of the single-stranded RCA products, such as staining or stretching via a receding meniscus, with the option of simultaneous (fluorescence) microscopic observation. It is shown that the stretched and surface-attached RCA products are accessible for hybridization of complementary oligonucleotides, which demonstrates their addressability by complementary base pairing. The long RCA products should be well suited to bridge the gap between biomolecular nanoscale building-blocks and structures at the micro- and macroscale, especially at the single- molecule level presented here.}, language = {en} } @article{GriessnerHartigChristmannetal.2010, author = {Grießner, Matthias and Hartig, Dave and Christmann, Alexander and Ehrentreich-F{\"o}rster, Eva and Warsinke, Axel and Bier, Frank Fabian}, title = {Surface regeneration of microfluidic microarray printheads through plasma techniques}, issn = {0960-1317}, doi = {10.1088/0960-1317/20/3/037002}, year = {2010}, abstract = {This work describes a method for surface regeneration of microfluidic microarray printheads through plasma techniques. Modification procedures were chosen in a way to obtain high reproducibility with a minimum of time consumption. The idea behind this is a complete regeneration of a microarray printhead before or after usage to achieve best printing results over a typical print job. A sequence of low-pressure oxygen-plasma and plasma polymerization with hexamethyldisiloxane (HMDSO) was used to regenerate printheads. Proof of the concept is given through quality control performed with a spotter implemented CCD camera, contact angle measurements and a typical hybridization experiment. Stable printing results were obtained over 3000 activations showing that the presented method is suitable for treatment of microarray printheads.}, language = {en} } @article{HuettlHettrichMilleretal.2013, author = {H{\"u}ttl, Christine and Hettrich, Cornelia and Miller, Reinhard and Paulke, Bernd-Reiner and Henklein, Petra and Rawel, Harshadrai Manilal and Bier, Frank Fabian}, title = {Self-assembled peptide amphiphiles function as multivalent binder with increased hemagglutinin affinity}, series = {BMC biotechnology}, volume = {13}, journal = {BMC biotechnology}, number = {22}, publisher = {BioMed Central}, address = {London}, issn = {1472-6750}, doi = {10.1186/1472-6750-13-51}, pages = {10}, year = {2013}, abstract = {Background: A promising way in diagnostic and therapeutic applications is the development of peptide amphiphiles (PAs). Peptides with a palmitic acid alkylchain were designed and characterized to study the effect of the structure modifications on self-assembling capabilities and the multiple binding capacity to hemagglutinin (HA), the surface protein of influenza virus type A. The peptide amphiphiles consists of a hydrophilic headgroup with a biological functionality of the peptide sequence and a chemically conjugated hydrophobic tail. In solution they self-assemble easily to micelles with a hydrophobic core surrounded by a closely packed peptide-shell. Results: In this study the effect of a multiple peptide binding partner to the receptor binding site of HA could be determined with surface plasmon resonance measurements. The applied modification of the peptides causes signal amplification in relationship to the unmodified peptide wherein the high constant specificity persists. The molecular assembly of the peptides was characterized by the determination of critical micelle concentration (CMC) with concentration of 10(-5) M and the colloidal size distribution. Conclusion: The modification of the physico-chemical parameters by producing peptide amphiphiles form monomeric structures which enhances the binding affinity and allows a better examination of the interaction with the virus surface protein hemagglutinin.}, language = {en} }