@article{MertensHilschHaralampievetal.2018,
  author    = {Mertens, Monique and Hilsch, Malte and Haralampiev, Ivan and Volkmer, Rudolf and Wessig, Pablo and M{\"u}ller, Peter},
  title     = {Synthesis and characterization of a new Bifunctionalized, Fluorescent, and Amphiphilic molecule for recruiting SH-Containing molecules to membranes},
  series = {ChemBioChem},
  volume    = {19},
  journal   = {ChemBioChem},
  number    = {15},
  publisher = {Wiley-VCH},
  address   = {Weinheim},
  issn      = {1439-4227},
  doi       = {10.1002/cbic.201800268},
  pages     = {1643 -- 1647},
  year      = {2018},
  abstract  = {This study describes the synthesis and characterization of an amphiphilic construct intended to recruit SH-containing molecules to membranes. The construct consists of 1)an aliphatic chain to enable anchoring within membranes, 2)a maleimide moiety to react with the sulfhydryl group of a soluble (bio)molecule, and 3)a fluorescence moiety to allow the construct to be followed by fluorescence spectroscopy and microscopy. It is shown that the construct can be incorporated into preformed membranes, thus allowing application of the approach with biological membranes. The close proximity between the fluorophore and the maleimide moiety within the construct causes fluorescence quenching. This allows monitoring of the reaction with SH-containing molecules by measurement of increases in fluorescence intensity and lifetime. Notably, the construct distributes into laterally ordered membrane domains of lipid vesicles, which is probably triggered by the length of its membrane anchor. The advantages of the new construct can be employed for several biological, biotechnological, and medicinal applications.},
  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{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-F{\"o}rster, Eva and Bier, Frank Fabian and St{\"o}cklein, Walter F. M.},
  title     = {Anti-hemagglutinin antibody derived lead peptides for inhibitors of influenza virus binding},
  series = {Postprints der Universit{\"a}t Potsdam : Mathematisch-Naturwissenschaftliche Reihe},
  journal   = {Postprints der Universit{\"a}t Potsdam : Mathematisch-Naturwissenschaftliche Reihe},
  number    = {536},
  issn      = {1866-8372},
  doi       = {10.25932/publishup-41087},
  url       = {http://nbn-resolving.de/urn:nbn:de:kobv:517-opus4-410872},
  pages     = {24},
  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}
}
@article{HaralampievMertensSchwarzeretal.2015,
  author    = {Haralampiev, Ivan and Mertens, Monique and Schwarzer, Roland and Herrmann, Andreas and Volkmer, Rudolf and Wessig, Pablo and Mueller, Peter},
  title     = {Recruitment of SH-Containing peptides to lipid and biological membranes through the use of a palmitic acid functionalized with a Maleimide Group},
  series = {Angewandte Chemie : a journal of the Gesellschaft Deutscher Chemiker ; International edition},
  volume    = {54},
  journal   = {Angewandte Chemie : a journal of the Gesellschaft Deutscher Chemiker ; International edition},
  number    = {1},
  publisher = {Wiley-VCH},
  address   = {Weinheim},
  issn      = {1433-7851},
  doi       = {10.1002/anie.201408089},
  pages     = {323 -- 326},
  year      = {2015},
  abstract  = {This study presents a novel and easily applicable approach to recruit sulfhydryl-containing biomolecules to membranes by using a palmitic acid which is functionalized with a maleimide group. Notably, this strategy can also be employed with preformed (biological) membranes. The applicability of the assay is demonstrated by characterizing the binding of a Rhodamine-labeled peptide to lipid and cellular membranes using methods of fluorescence spectroscopy, lifetime measurement, and microscopy. Our approach offers new possibilities for preparing biologically active liposomes and manipulating living cells.},
  language  = {en}
}
@inproceedings{HaralampievMertensSchwarzeretal.2015,
  author    = {Haralampiev, Ivan and Mertens, Monique and Schwarzer, Roland and Herrmann, Andreas and Volkmer, Rudolf and Wessig, Pablo and M{\"u}ller, Peter},
  title     = {A palmitic acid functionalized with a maleimide group is used to recruit SH-containing peptides to lipid and biological membranes},
  series = {The FEBS journal},
  volume    = {282},
  booktitle = {The FEBS journal},
  publisher = {Wiley-Blackwell},
  address   = {Hoboken},
  issn      = {1742-464X},
  pages     = {204 -- 204},
  year      = {2015},
  language  = {en}
}
@article{DaskalowBoisguerinJandrigetal.2010,
  author    = {Daskalow, Katjana and Boisguerin, Prisca and Jandrig, Burkhard and van Landeghem, Frank K. H. and Volkmer, Rudolf and Micheel, Burkhard and Schenk, J{\"o}rg A.},
  title     = {Generation of an antibody against the protein phosphatase 1 inhibitor KEPI and characterization of the epitope},
  issn      = {0250-7005},
  year      = {2010},
  abstract  = {A monoclonal antibody against the potential tumor suppressor kinase-enhanced protein phosphatase 1 (PP1) inhibitor KEPI (PPP1R14C) was generated and characterized. Human KEPI was expressed in Escherichia coli and used to immunize Balb/c mice. Using hybridoma technology, one clone, G18AF8, was isolated producing antibodies which bound specifically to the KEPI protein in ELISA, immunoblotting and flow cytometry. The antibody was also successfully applied to stain KEPI protein in paraffin sections of human brain. The epitope was mapped using peptide array technology and confirmed as GARVFFQSPR. This corresponds to the N-terminal region of KEPI. Amino acid substitution analysis revealed that two residues, F and Q, are essential for binding. Affinity of binding was determined by competitive ELISA as 1 mu M. In Western blot assays testing G18AF8 antibody on brain samples of several species, reactivity with hamster, rat and chicken samples was found, suggesting a broad homology of this KEPI epitope in vertebrates. This antibody could be used in expression studies at the protein level e.g. in tumor tissues.},
  language  = {en}
}