@article{BaderKlierHettrichetal.2016,
  author    = {Bader, Denise and Klier, Dennis Tobias and Hettrich, C. and Bier, Frank Fabian and Wessig, Pablo},
  title     = {Detecting carbohydrate-lectin interactions using a fluorescent probe based on DBD dyes},
  series = {Analytical methods : advancing methods and applications},
  volume    = {8},
  journal   = {Analytical methods : advancing methods and applications},
  publisher = {Royal Society of Chemistry},
  address   = {Cambridge},
  issn      = {1759-9660},
  doi       = {10.1039/c5ay02991k},
  pages     = {1235 -- 1238},
  year      = {2016},
  abstract  = {Herein we present an efficient synthesis of a biomimetic probe with modular construction that can be specifically bound by the mannose binding FimH protein - a surface adhesion protein of E. coli bacteria. The synthesis combines the new and interesting DBD dye with the carbohydrate ligand mannose via a Click reaction. We demonstrate the binding to E. coli bacteria over a large concentration range and also present some special characteristics of those molecules that are of particular interest for the application as a biosensor. In particular, the mix-and-measure ability and the very good photo-stability should be highlighted here.},
  language  = {en}
}
@article{ConnorZantowHustetal.2016,
  author    = {Connor, Daniel Oliver and Zantow, Jonas and Hust, Michael and Bier, Frank Fabian and von Nickisch-Rosenegk, Markus},
  title     = {Identification of Novel Immunogenic Proteins of Neisseria gonorrhoeae by Phage Display},
  series = {PLoS one},
  volume    = {11},
  journal   = {PLoS one},
  publisher = {PLoS},
  address   = {San Fransisco},
  issn      = {1932-6203},
  doi       = {10.1371/journal.pone.0148986},
  pages     = {24},
  year      = {2016},
  abstract  = {Neisseria gonorrhoeae is one of the most prevalent sexually transmitted diseases worldwide with more than 100 million new infections per year. A lack of intense research over the last decades and increasing resistances to the recommended antibiotics call for a better understanding of gonococcal infection, fast diagnostics and therapeutic measures against N. gonorrhoeae. Therefore, the aim of this work was to identify novel immunogenic proteins as a first step to advance those unresolved problems. For the identification of immunogenic proteins, pHORF oligopeptide phage display libraries of the entire N. gonorrhoeae genome were constructed. Several immunogenic oligopeptides were identified using polyclonal rabbit antibodies against N. gonorrhoeae. Corresponding full-length proteins of the identified oligopeptides were expressed and their immunogenic character was verified by ELISA. The immunogenic character of six proteins was identified for the first time. Additional 13 proteins were verified as immunogenic proteins in N. gonorrhoeae.},
  language  = {en}
}
@article{MemczakLausterKaretal.2016,
  author    = {Memczak, Henry and Lauster, Daniel and Kar, Parimal and Di Lella, Santiago and Volkmer, Rudolf and Knecht, Volker and Herrmann, Andreas and Ehrentreich-Foerster, Eva and Bier, Frank Fabian and Stoecklein, Walter F. M.},
  title     = {Anti-Hemagglutinin Antibody Derived Lead Peptides for Inhibitors of Influenza Virus Binding},
  series = {PLoS one},
  volume    = {11},
  journal   = {PLoS one},
  publisher = {PLoS},
  address   = {San Fransisco},
  issn      = {1932-6203},
  doi       = {10.1371/journal.pone.0159074},
  pages     = {82 -- 90},
  year      = {2016},
  abstract  = {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.},
  language  = {en}
}
@misc{WessigBaderKlieretal.2016,
  author    = {Wessig, Pablo and Bader, Denise and Klier, Dennis Tobias and Hettrich, Cornelia and Bier, Frank Fabian},
  title     = {Detecting carbohydrate-lectin interactions using a fluorescent probe based on DBD dyes},
  url       = {http://nbn-resolving.de/urn:nbn:de:kobv:517-opus4-394382},
  pages     = {1235 -- 1238},
  year      = {2016},
  abstract  = {Herein we present an efficient synthesis of a biomimetic probe with modular construction that can be specifically bound by the mannose binding FimH protein - a surface adhesion protein of E. coli bacteria. The synthesis combines the new and interesting DBD dye with the carbohydrate ligand mannose via a Click reaction. We demonstrate the binding to E. coli bacteria over a large concentration range and also present some special characteristics of those molecules that are of particular interest for the application as a biosensor. In particular, the mix-and-measure ability and the very good photo-stability should be highlighted here.},
  language  = {en}
}