TY - JOUR A1 - Himmel, Mirko A1 - VanderVen, Peter F. M. A1 - Stöcklein, Walter F. M. A1 - Fürst, Dieter Oswald T1 - The limits of promiscuity : isoform-specific dimerization of filamins Y1 - 2003 ER - TY - JOUR A1 - Lisdat, Fred A1 - Utepbergenov, D. A1 - Haseloff, R. F. A1 - Blasig, Ingolf E. A1 - Stöcklein, Walter F. M. A1 - Scheller, Frieder W. A1 - Brigelius-Flohé, Regina T1 - An optical method for the detection of oxidative stress using protein-RNA interaction Y1 - 2001 ER - TY - JOUR A1 - Stöcklein, Walter F. M. A1 - Rohde, M. A1 - Scharte, Gudrun A1 - Behrsing, Olaf A1 - Warsinke, Axel A1 - Micheel, Burkhard A1 - Scheller, Frieder W. T1 - Sensitive detection of triazine and phenylurea pesticides in pure organic solvent by enzyme linked immunsorbent assay (ELISA): stabilities, solubilities and sensitives Y1 - 2000 ER - TY - JOUR A1 - Nitsche, Andreas A1 - Kurth, Andreas A1 - Dunkhorst, Anna A1 - Pänke, Oliver A1 - Sielaff, Hendrik A1 - Junge, Wolfgang A1 - Muth, Doreen A1 - Scheller, Frieder W. A1 - Stöcklein, Walter F. M. A1 - Pauli, Georg A1 - Kage, Andreas T1 - One-step selection of vaccinia virus binding DNA-aptamers by MonoLEX Y1 - 2007 UR - http://www.biomedcentral.com/1472-6750/7 U6 - https://doi.org/10.1186/1472-6750-7-48 ER - TY - JOUR A1 - Neumann, Meina A1 - Schulte, Marc A1 - Jünemann, Nora A1 - Stöcklein, Walter F. M. A1 - Leimkühler, Silke T1 - Rhodobacter capsulatus XdhC is involved in molybdenum cofactor binding and insertion into xanthine dehydrogenase N2 - Rhodobacter capsulatus xanthine dehydrogenase (XDH) is a cytoplasmic enzyme with an (alpha beta) 2 heterodimeric structure that is highly identical to homodimeric eukaryotic xanthine oxidoreductases. The crystal structure revealed that the molybdenum cofactor (Moco) is deeply buried within the protein. A protein involved in Moco insertion and XDH maturation has been identified, which was designated XdhC. XdhC was shown to be essential for the production of active XDH but is not a subunit of the purified enzyme. Here we describe the purification of XdhC and the detailed characterization of its role for XDH maturation. We could show that XdhC binds Moco in stoichiometric amounts, which subsequently can be inserted into Moco-free apo-XDH. A specific interaction between XdhC and XdhB was identified. We show that XdhC is required for the stabilization of the sulfurated form of Moco present in enzymes of the xanthine oxidase family. Our findings imply that enzyme-specific proteins exist for the biogenesis of molybdoenzymes, coordinating Moco binding and insertion into their respective target proteins. So far, the requirement of such proteins for molybdoenzyme maturation has been described only for prokaryotes Y1 - 2006 UR - http://www.jbc.org/ U6 - https://doi.org/10.1074/jbc.M601617200 ER - TY - JOUR A1 - Beissenhirtz, Moritz Karl A1 - Scheller, Frieder W. A1 - Stöcklein, Walter F. M. A1 - Kurth, D. A1 - Möhwald, Helmuth A1 - Lisdat, Fred T1 - Electroactive cytochrome c multilayers within a polyelectrolyte assembly Y1 - 2004 ER - TY - JOUR A1 - Stöcklein, Walter F. M. T1 - Molecule-detective BT - Molekül-Detektive : Biosensoren N2 - Biosensors are analytical devices incorporating biological material (receptor) intimately associated with or integrated within a physicochernical transducer. Advantages are the high selectivity for analyte detection. Examples given comprise the very successful commercial blood glucose biosensors made for the self-control by the diabetic patients. Other biosensors are part of an analytic system, including the sensor chips Of surface plasmon resonance or interferometry based devices, piezoelectric or reflectometric sensors capable of direct measurement of mass changes, and thermometric and other reagentless sensors. The development of nanotubes-based devices allows for significant enhancment of the signal-to-noise ratio of the biosensors. A milestone on the way towards miniaturization and parallelization of biosensors is the recently developed and prize-winning electronic DNA chip Y1 - 2006 ER - TY - JOUR A1 - Liu, Songqin A1 - Wollenberger, Ursula A1 - Halamek, Jan A1 - Leupold, Eik A1 - Stöcklein, Walter F. M. A1 - Warsinke, Axel A1 - Scheller, Frieder W. T1 - Affinity interaction betwen phenylboronic acid-carrying self-assembled monolayers and FAD or HRP N2 - A method is provided for the recognition of glycated molecules based on their binding affinities to boronate- carrying monolayers. The affinity interaction of flavin adenine dinucleotide (FAD) and horseradish peroxidase (HRP) with phenylboronic acid monolayers on gold was investigated by using voltammetric and microgravimetric methods. Conjugates of 3-aminopherrylboronic acid and 3,3'-dithiodipropionic acid di(N-hydroxysuccinimide ester) or 11-mercaptoundecanoic acid were prepared and self-assembled on gold surfaces to generate monolayers. FAD is bound to this modified sur-face and recognized by a pair of redox peaks with a formal potential of -0.433 V in a 0.1 m phosphate buffer solution, pH 6.5. Upon addition of a sugar to the buffer, the bound FAD could be replaced, indicating that the binding is reversible. Voltammetric, mass measurements, and photometric activity assays show that the HRP can also be bound to the interface. This binding is reversible, and HRP can be replaced by sorbitol or removed in acidic solution. The effects of pH, incubation time, and concentration of H2O2 were studied by comparing the catalytic reduction of H2O2 in the presence of the electron-donor thionine. The catalytic current of the HRP-loaded electrode was proportional to HRP concentrations in the incubation solution in the range between 5 mu g mL(-1) and 0.4 mg mL(-1) with a linear slope of 3.34 mu A mL mg(-1) and a correlation coefficient of 0.9945 Y1 - 2005 ER - TY - JOUR A1 - Kleuser, U. A1 - Stöcklein, Walter F. M. A1 - Pieper-Fürst, U. A1 - Scheller, Frieder W. T1 - Partikelverstärkte Oberflächenplasmonresonanz für die Quantifizierung von Matrix Metalloproteinase-2 Y1 - 2004 ER - TY - JOUR A1 - Pieper-Fürst, U. A1 - Kleuser, U. A1 - Stöcklein, Walter F. M. A1 - Warsinke, Axel A1 - Scheller, Frieder W. T1 - Detection of subicomolar concentrations of human matrix metalloproteinase-2 by an optical biosensor N2 - We describe in this paper the development of a one-step sandwich assay for the highly sensitive and fast detection of human matrix metalloproteinase (MMP)-2 (EC 3.4.24.24), using surface plasmon resonance (SPR). For the assay, two ligands were selected: monoclonal anti-MMP-2 antibody Ab-2 and the tissue inhibitor of metalloproteinases (TIMP)-2. They were chosen on the basis of (1) their affinities to MMP-2, (2) the efficiency of immobilization to the sensor chip, (3) the efficiency of adsorption to colloidal gold, and (4) the stability of these protein-coated gold particles. The assay included mixing of MMP-2 with antibody Ab-2 adsorbed to colloidal gold with a diameter of about 20 rim and injection into the flowcell of the SPR instrument containing immobilized TIMP-2. By using colloidal gold particles an amplification factor of 114 and a detection limit of 0.5 pM for MMP-2 were obtained. The precision of the assay was high even at low analyte concentrations, the standard deviation being 8.3% for five determinations of 1 pM MMP- 2. No significant binding was observed with the structurally related MMP-9. The assay is far more sensitive and faster than commonly used methods for MMP-2 detection. As TIMP-bound MMP-2 is not detected by this method, the assay can be applied for measuring free MMP-2, reflecting the imbalance of free and inhibitor-bound enzyme in various pathological situations. (C) 2004 Elsevier Inc. All rights reserved Y1 - 2004 ER - TY - JOUR A1 - Chen, Jian A1 - Stöcklein, Walter F. M. A1 - Scheller, Frieder W. A1 - Wollenberger, Ursula T1 - Electrochemical determination of human hemoglobin by using ferrocene carboxylic acid modified carbon powder microelectrode Y1 - 2003 ER - TY - JOUR A1 - Nießner, Reinhard A1 - Broekaert, J. A1 - Einax, J. W. A1 - Scheller, Frieder W. A1 - Stöcklein, Walter F. M. T1 - Trendbericht analytische Biochemie 2000/2001 Y1 - 2002 ER - TY - JOUR A1 - Sass, Stephan A1 - Stöcklein, Walter F. M. A1 - Klevesath, Anja A1 - Hurpin, Jeanne A1 - Menger, Marcus A1 - Hille, Carsten T1 - Binding affinity data of DNA aptamers for therapeutic anthracyclines from microscale thermophoresis and surface plasmon resonance spectroscopy JF - The analyst : the analytical journal of the Royal Society of Chemistry N2 - Anthracyclines like daunorubicin (DRN) and doxorubicin (DOX) play an undisputed key role in cancer treatment, but their chronic administration can cause severe side effects. For precise anthracycline analytical systems, aptamers are preferable recognition elements. Here, we describe the detailed characterisation of a single-stranded DNA aptamer DRN-10 and its truncated versions for DOX and DRN detection. Binding affinities were determined from surface plasmon resonance (SPR) and microscale thermophoresis (MST) and combined with conformational data from circular dichroism (CD). Both aptamers displayed similar nanomolar binding affinities to DRN and DOX, even though their rate constants differed as shown by SPR recordings. SPR kinetic data unravelled a two-state reaction model including a 1 : 1 binding and a subsequent conformational change of the binding complex. This model was supported by CD spectra. In addition, the dissociation constants determined with MST were always lower than that from SPR, and especially for the truncated aptamer they differed by two orders of magnitude. This most probably reflects the methodological difference, namely labelling for MST vs. immobilisation for SPR. From CD recordings, we suggested a specific G-quadruplex as structural basis for anthracycline binding. We concluded that the aptamer DRN-10 is a promising recognition element for anthracycline detection systems and further selected aptamers can be also characterised with the combined methodological approach presented here. Y1 - 2019 U6 - https://doi.org/10.1039/c9an01247h SN - 0003-2654 SN - 1364-5528 VL - 144 IS - 20 SP - 6064 EP - 6073 PB - Royal Society of Chemistry CY - Cambridge ER - TY - JOUR A1 - Stöcklein, Walter F. M. A1 - Makower, Alexander A1 - Bier, Frank Fabian A1 - Scheller, Frieder W. T1 - Enzyme sensors and enzyme amplifification systems Y1 - 1997 ER - TY - JOUR A1 - Hovestaedt, Marc A1 - Memczak, Henry A1 - Pleiner, Dennis A1 - Zhang, Xin A1 - Rappich, Joerg A1 - Bier, Frank Fabian A1 - Stöcklein, Walter F. M. T1 - Characterization of a new maleimido functionalization of gold for surface plasmon resonance spectroscopy JF - Journal of molecular recognition : an international journal devoted to research on specific molecular recognition in chemistry, biology, biotechnology and medicine N2 - Para-maleimidophenyl (p-MP) modified gold surfaces have been prepared by one-step electrochemical deposition and used in surface plasmon resonance (SPR) studies. Therefore, a FITC mimotope peptide (MP1, 12 aa), a human mucin 1 epitope peptide (MUC, 9 aa) and a protein with their specific antibodies were used as model systems. The peptides were modified with an N-terminal cysteine for covalent and directed coupling to the maleimido functionalized surface by means of Michael addition. The coupling yield of the peptide, the binding characteristics of antibody and the unspecific adsorption of the analytes were investigated. The results expand the spectrum of biosensors usable with p-MP by widely used SPR and support its potential to be versatile for several electrochemical and optical biosensors. This allows the combination of an electrochemical and optical read-out for a broad variety of biomolecular interactions on the same chip. Copyright (c) 2014 John Wiley & Sons, Ltd. KW - biosensor KW - surface plasmon resonance KW - diazonium coupling KW - maleimidophenyl KW - cys-peptide KW - aryl diazonium salts Y1 - 2014 U6 - https://doi.org/10.1002/jmr.2396 SN - 0952-3499 SN - 1099-1352 VL - 27 IS - 12 SP - 707 EP - 713 PB - Wiley-Blackwell CY - Hoboken ER - TY - GEN A1 - Memczak, Henry A1 - Lauster, Daniel A1 - Kar, Parimal A1 - Di Lella, Santiago A1 - Volkmer, Rudolf A1 - Knecht, Volker A1 - Herrmann, Andreas A1 - Ehrentreich-Förster, Eva A1 - Bier, Frank Fabian A1 - Stöcklein, Walter F. M. T1 - Anti-hemagglutinin antibody derived lead peptides for inhibitors of influenza virus binding T2 - Postprints der Universität Potsdam : Mathematisch-Naturwissenschaftliche Reihe N2 - Antibodies against spike proteins of influenza are used as a tool for characterization of viruses and therapeutic approaches. However, development, production and quality control of antibodies is expensive and time consuming. To circumvent these difficulties, three peptides were derived from complementarity determining regions of an antibody heavy chain against influenza A spike glycoprotein. Their binding properties were studied experimentally, and by molecular dynamics simulations. Two peptide candidates showed binding to influenza A/Aichi/2/68 H3N2. One of them, termed PeB, with the highest affinity prevented binding to and infection of target cells in the micromolar region without any cytotoxic effect. PeB matches best the conserved receptor binding site of hemagglutinin. PeB bound also to other medical relevant influenza strains, such as human-pathogenic A/California/7/2009 H1N1, and avian-pathogenic A/MuteSwan/Rostock/R901/2006 H7N1. Strategies to improve the affinity and to adapt specificity are discussed and exemplified by a double amino acid substituted peptide, obtained by substitutional analysis. The peptides and their derivatives are of great potential for drug development as well as biosensing. T3 - Zweitveröffentlichungen der Universität Potsdam : Mathematisch-Naturwissenschaftliche Reihe - 536 KW - receptor-binding KW - A viruses KW - neutralizing antibody KW - avian influenza KW - origin KW - neuraminidase KW - invection KW - entry KW - sites KW - identification Y1 - 2019 U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:kobv:517-opus4-410872 SN - 1866-8372 IS - 536 ER - TY - CHAP A1 - Memczak, Henry A1 - Lauster, Daniel A1 - Herrmann, Andreas A1 - Stöcklein, Walter F. M. A1 - Bier, Frank Fabian T1 - Novel hemagglutinin-binding peptides for biosensing and inhibition of Influenza Viruses T2 - Biopolymers Y1 - 2013 SN - 0006-3525 SN - 1097-0282 VL - 100 IS - 3 SP - 255 EP - 255 PB - Wiley-Blackwell CY - Hoboken ER - TY - JOUR A1 - Stöcklein, Walter F. M. A1 - Warsinke, Axel A1 - Scheller, Frieder W. T1 - Organic solvent modified enzyme-liked immunoassay for the detection of triazine herbicides Y1 - 1997 ER - TY - JOUR A1 - Stöcklein, Walter F. M. A1 - Scheller, Frieder W. T1 - Enzymes and antibodies in organic media : analytical applications Y1 - 1997 ER - TY - JOUR A1 - Kramer, A. A1 - Keitel, T. A1 - Winkler, K. A1 - Stöcklein, Walter F. M. A1 - Hühne, Wolfgang A1 - Schneider-Mergener, Jens T1 - Molecular basis for the binding promiscuity of an anti-P24 (HIV-1) monoclonal antibody Y1 - 1997 ER -