TY - JOUR A1 - Wawrzinek, Robert A1 - Ziomkowska, Joanna A1 - Heuveling, Johanna A1 - Mertens, Monique A1 - Herrmann, Andreas A1 - Schneider, Erwin A1 - Wessig, Pablo T1 - DBD Dyes as Fluorescence Lifetime Probes to Study Conformational Changes in Proteins JF - CHEMISTRY-A EUROPEAN JOURNAL N2 - Previously, [1,3]dioxolo[4,5-f][1,3]benzodioxole (DBD)-based fluorophores used as highly sensitive fluorescence lifetime probes reporting on their microenvironmental polarity have been described. Now, a new generation of DBD dyes has been developed. Although they are still sensitive to polarity, in contrast to the former DBD dyes, they have extraordinary spectroscopic properties even in aqueous surroundings. They are characterized by long fluorescence lifetimes (10-20ns), large Stokes shifts (approximate to 100nm), high photostabilities, and high quantum yields (>0.56). Here, the spectroscopic properties and synthesis of functionalized derivatives for labeling biological targets are described. Furthermore, thio-reactive maleimido derivatives of both DBD generations show strong intramolecular fluorescence quenching. This mechanism has been investigated and is found to undergo a photoelectron transfer (PET) process. After reaction with a thiol group, this fluorescence quenching is prevented, indicating successful bonding. Being sensitive to their environmental polarity, these compounds have been used as powerful fluorescence lifetime probes for the investigation of conformational changes in the maltose ATP-binding cassette transporter through fluorescence lifetime spectroscopy. The differing tendencies of the fluorescence lifetime change for both DBD dye generations promote their combination as a powerful toolkit for studying microenvironments in proteins. KW - dyes KW - pigments KW - electron transfer KW - fluorescent probes KW - maleimides KW - MalF KW - photoelectron transfer Y1 - 2013 U6 - https://doi.org/10.1002/chem.201302368 SN - 0947-6539 SN - 1521-3765 VL - 19 IS - 51 SP - 17349 EP - 17357 PB - WILEY-V C H VERLAG GMBH CY - WEINHEIM ER - TY - JOUR A1 - Wawrzinek, Robert A1 - Wessig, Pablo A1 - Möllnitz, Kristian A1 - Nikolaus, Joerg A1 - Schwarzer, Roland A1 - Müller, Peter A1 - Herrmann, Andreas T1 - DBD dyes as fluorescent probes for sensing lipophilic environments JF - Bioorganic & medicinal chemistry letters : a Tetrahedron publication for rapid dissemination of preliminary communications on all aspects of bioorganic chemistry, medicinal chemistry and related disciplines N2 - Small fluorescent organic molecules based on [1,3]dioxolo[4,5-f][1,3]benzodioxole (DBD) could be used as probes for lipophillic microenvironments in aqueous solutions by indicating the critical micelles concentration of detergents and staining cell organelles. Their fluorescence lifetime decreases drastically by the amount of water in their direct environment. Therefore they are potential probes for fluorescence lifetime imaging microscopy (FLIM). KW - Fluorescence lifetime probes KW - FLIM KW - Cell staining KW - Lysotrackers KW - Detergents Y1 - 2012 U6 - https://doi.org/10.1016/j.bmcl.2012.07.056 SN - 0960-894X VL - 22 IS - 17 SP - 5367 EP - 5371 PB - Elsevier CY - Oxford ER - TY - JOUR A1 - Sperber, Hannah Sabeth A1 - Welke, Robert-William A1 - Petazzi, Roberto Arturo A1 - Bergmann, Ronny A1 - Schade, Matthias A1 - Shai, Yechiel A1 - Chiantia, Salvatore A1 - Herrmann, Andreas A1 - Schwarzer, Roland T1 - Self-association and subcellular localization of Puumala hantavirus envelope proteins JF - Scientific reports N2 - Hantavirus assembly and budding are governed by the surface glycoproteins Gn and Gc. In this study, we investigated the glycoproteins of Puumala, the most abundant Hantavirus species in Europe, using fluorescently labeled wild-type constructs and cytoplasmic tail (CT) mutants. We analyzed their intracellular distribution, co-localization and oligomerization, applying comprehensive live, single-cell fluorescence techniques, including confocal microscopy, imaging flow cytometry, anisotropy imaging and Number&Brightness analysis. We demonstrate that Gc is significantly enriched in the Golgi apparatus in absence of other viral components, while Gn is mainly restricted to the endoplasmic reticulum (ER). Importantly, upon co-expression both glycoproteins were found in the Golgi apparatus. Furthermore, we show that an intact CT of Gc is necessary for efficient Golgi localization, while the CT of Gn influences protein stability. Finally, we found that Gn assembles into higher-order homo-oligomers, mainly dimers and tetramers, in the ER while Gc was present as mixture of monomers and dimers within the Golgi apparatus. Our findings suggest that PUUV Gc is the driving factor of the targeting of Gc and Gn to the Golgi region, while Gn possesses a significantly stronger self-association potential. Y1 - 2019 U6 - https://doi.org/10.1038/s41598-018-36879-y SN - 2045-2322 VL - 9 PB - Nature Publ. Group CY - London ER - TY - GEN A1 - Sperber, Hannah Sabeth A1 - Welke, Robert-William A1 - Petazzi, Roberto Arturo A1 - Bergmann, Ronny A1 - Schade, Matthias A1 - Shai, Yechiel A1 - Chiantia, Salvatore A1 - Herrmann, Andreas A1 - Schwarzer, Roland T1 - Self-association and subcellular localization of Puumala hantavirus envelope proteins T2 - Postprints der Universität Potsdam : Mathematisch-Naturwissenschaftliche Reihe N2 - Hantavirus assembly and budding are governed by the surface glycoproteins Gn and Gc. In this study, we investigated the glycoproteins of Puumala, the most abundant Hantavirus species in Europe, using fluorescently labeled wild-type constructs and cytoplasmic tail (CT) mutants. We analyzed their intracellular distribution, co-localization and oligomerization, applying comprehensive live, single-cell fluorescence techniques, including confocal microscopy, imaging flow cytometry, anisotropy imaging and Number&Brightness analysis. We demonstrate that Gc is significantly enriched in the Golgi apparatus in absence of other viral components, while Gn is mainly restricted to the endoplasmic reticulum (ER). Importantly, upon co-expression both glycoproteins were found in the Golgi apparatus. Furthermore, we show that an intact CT of Gc is necessary for efficient Golgi localization, while the CT of Gn influences protein stability. Finally, we found that Gn assembles into higher-order homo-oligomers, mainly dimers and tetramers, in the ER while Gc was present as mixture of monomers and dimers within the Golgi apparatus. Our findings suggest that PUUV Gc is the driving factor of the targeting of Gc and Gn to the Golgi region, while Gn possesses a significantly stronger self-association potential. T3 - Zweitveröffentlichungen der Universität Potsdam : Mathematisch-Naturwissenschaftliche Reihe - 648 KW - Sin-Nombre-Virus KW - nucleocapsid protein KW - cytoplasmic tails KW - electron cryotomography KW - autophagic clearance KW - glycoprotein KW - Gn KW - G1 KW - brightness KW - fever Y1 - 2019 U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:kobv:517-opus4-425040 SN - 1866-8372 IS - 648 ER - TY - JOUR A1 - Ristow, Michael A1 - Herrmann, Andreas A1 - Illig, Hubert A1 - Klemm, Gunther A1 - Kummer, Volker A1 - Kläge, Hans-Christian A1 - Machatzi, Bernd A1 - Raetzel, Stefan A1 - Schwarz, R. A1 - Zimmermann, Friedrich T1 - Liste und Rote Liste der etablierten Gefäßpflanzen Brandenburgs Y1 - 2006 ER - TY - JOUR A1 - Nikolaus, Jörg A1 - Czapla, Sylvia A1 - Möllnitz, Kristian A1 - Höfer, Chris T. A1 - Herrmann, Andreas A1 - Wessig, Pablo A1 - Müller, Peter T1 - New molecular rods - Characterization of their interaction with membranes JF - Biochimica et biophysica acta : Biomembranes N2 - Molecular rods are synthetical molecules consisting of a hydrophobic backbone which are functionalized with varying terminal groups. Here, we report on the interaction of a recently described new class of molecular rods with lipid and biological membranes. In order to characterize this interaction, different fluorescently labeled rods were synthesized allowing for the application of fluorescence spectroscopy and microscopy based approaches. Our data show that the rods are incorporated into membranes with a perpendicular orientation to the membrane surface and enrich preferentially in liquid-disordered lipid domains. These characteristics underline that rods can be applied as stable membrane-associated anchors for functionalizing membrane surfaces. KW - Molecular rod KW - Phospholipid KW - Lipid domain KW - Spiro compound Y1 - 2011 U6 - https://doi.org/10.1016/j.bbamem.2011.08.008 SN - 0005-2736 VL - 1808 IS - 12 SP - 2781 EP - 2788 PB - Elsevier CY - Amsterdam ER - TY - JOUR A1 - Müller, Peter A1 - Nikolaus, Jörg A1 - Schiller, Sabine A1 - Herrmann, Andreas A1 - Moellnitz, Kristian A1 - Czapla, Sylvia A1 - Wessig, Pablo T1 - Molecular rods with oligospiroketal backbones as anchors in biological membranes N2 - Getting stuck in: A hydrophobic molecular rod with terminal fluorescent moieties has been synthesized. The insertion of the rod into membranes was investigated and shown to incorporate efficiently into model and biological membranes (see picture; gray C, blue N, red O). Those rods can be used as stable membrane-associated anchors for functionalization of membrane surfaces. Y1 - 2009 UR - http://www3.interscience.wiley.com/cgi-bin/jhome/26737/ U6 - https://doi.org/10.1002/anie.200901133 SN - 1433-7851 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 - JOUR A1 - Memczak, Henry A1 - Lauster, Daniel A1 - Kar, Parimal A1 - Di Lella, Santiago A1 - Volkmer, Rudolf A1 - Knecht, Volker A1 - Herrmann, Andreas A1 - Ehrentreich-Foerster, Eva A1 - Bier, Frank Fabian A1 - Stoecklein, Walter F. M. T1 - Anti-Hemagglutinin Antibody Derived Lead Peptides for Inhibitors of Influenza Virus Binding JF - PLoS one 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. Y1 - 2016 U6 - https://doi.org/10.1371/journal.pone.0159074 SN - 1932-6203 VL - 11 SP - 82 EP - 90 PB - PLoS CY - San Fransisco 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 -