@article{EisoldSellrieMemczaketal.2018,
  author    = {Eisold, Ursula and Sellrie, Frank and Memczak, Henry and Andersson, Anika and Schenk, J{\"o}rg A. and Kumke, Michael Uwe},
  title     = {Dye tool box for a fluorescence enhancement immunoassay},
  series = {Bioconjugate chemistry},
  volume    = {29},
  journal   = {Bioconjugate chemistry},
  number    = {1},
  publisher = {American Chemical Society},
  address   = {Washington},
  issn      = {1043-1802},
  doi       = {10.1021/acs.bioconjchem.7b00731},
  pages     = {203 -- 214},
  year      = {2018},
  abstract  = {Immunochemical analytical methods are very successful in clinical diagnostics and are nowadays also emerging in the control of food as well as monitoring of environmental issues. Among the different immunoassays, luminescence based formats are characterized by their outstanding sensitivity making this format especially attractive for future applications. The need for multiparameter detection capabilities calls for a tool box of dye labels in order to transduce the biochemical reaction into an optically detectable signal. Here, in a multiparameter approach each analyte may be detected by a different dye with a unique emission color (covering the blue to red spectral range) or a unique luminescence decay kinetics. In the case of a competitive immunoassay format for each of the different dye labels an individual antibody would be needed. In the present paper a slightly modified approach is presented using a 7-aminocoumarin unit as the basic antigen against which highly specific antibodies were generated. Leaving the epitope region in the dyes unchanged but introducing a side group in positon 3 of the coumarin system allowed us to tune the optical properties of the coumarin dyes without the necessity of new antibody generation. Upon modification of the parent coumarin unit the full spectral range from blue to deep red was accessed. In the manuscript the photophysical characterization of the coumarin derivatives and their corresponding immunocomplexes with two highly specific antibodies is presented. The coumarin dyes and their immunocomplexes were characterized by steady-state and time-resolved absorption as well as emission spectroscopy. Moreover, fluorescence depolarization measurements were carried out to complement the data stressing the different binding modes of the two antibodies. The binding modes were evaluated using the photophysics of 7-aminocoumarins and how it was affected in the respective immunocomplexes, namely, the formation of the intramolecular charge transfer (ICT) as well as the twisted intramolecular charge transfer (TICT). In contrast to other antibody-dye pairs reported a distinct fluorescence enhancement upon formation of the antibody-dye complex up to a factor of SO was found. Because of the easy emission color tuning by tailoring the coumarin substitution for the antigen binding in nonrelevant position 3 of the parent molecule, a dye tool box is on hand which can be used in the construction of competitive multiparameter fluorescence enhancement immunoassays (FenIA).},
  language  = {en}
}
@article{HovestaedtMemczakPleineretal.2014,
  author    = {Hovestaedt, Marc and Memczak, Henry and Pleiner, Dennis and Zhang, Xin and Rappich, Joerg and Bier, Frank Fabian and St{\"o}cklein, Walter F. M.},
  title     = {Characterization of a new maleimido functionalization of gold for surface plasmon resonance spectroscopy},
  series = {Journal of molecular recognition : an international journal devoted to research on specific molecular recognition in chemistry, biology, biotechnology and medicine},
  volume    = {27},
  journal   = {Journal of molecular recognition : an international journal devoted to research on specific molecular recognition in chemistry, biology, biotechnology and medicine},
  number    = {12},
  publisher = {Wiley-Blackwell},
  address   = {Hoboken},
  issn      = {0952-3499},
  doi       = {10.1002/jmr.2396},
  pages     = {707 -- 713},
  year      = {2014},
  abstract  = {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.},
  language  = {en}
}
@phdthesis{Memczak2014,
  author    = {Memczak, Henry},
  title     = {Entwicklung influenzabindender Peptide f{\"u}r die Biosensorik},
  url       = {http://nbn-resolving.de/urn:nbn:de:kobv:517-opus-72470},
  school      = {Universit{\"a}t Potsdam},
  pages     = {X, 117},
  year      = {2014},
  abstract  = {Das Influenzavirus infiziert S{\"a}ugetiere und V{\"o}gel. Der erste Schritt im Infektionszyklus ist die Anbindung des Viruses {\"u}ber sein Oberfl{\"a}chenprotein H{\"a}magglutinin (HA) an Zuckerstrukturen auf Epithelzellen des respiratorischen Traktes im Wirtsorganismus. Aus den drei komplementarit{\"a}tsbestimmenden Regionen (complementarity determining regions, CDRs) der schweren Kette eines monoklonalen H{\"a}magglutinin-bindenden Antik{\"o}rpers wurden drei lineare Peptide abgeleitet. Die Bindungseigenschaften der drei Peptide wurden experimentell mittels Oberfl{\"a}chenplasmonenresonanzspektroskopie untersucht. Es zeigte sich, dass in {\"U}bereinstimmung mit begleitenden Molekulardynamik-Simulationen zwei der drei Peptide (PeB und PeC) analog zur Bindef{\"a}higkeit des Antik{\"o}rpers in der Lage sind, Influenzaviren vom Stamm X31 (H3N2 A/Aichi/2/1968) zu binden. Die Interaktion des Peptids PeB, welches potentiell mit der konservierten Rezeptorbindestelle im HA interagiert, wurde anschließend n{\"a}her charakterisiert. Die Detektion der Influenzaviren war unter geeigneten Immobilisationsbedingungen im diagnostisch relevanten Bereich m{\"o}glich. Die Spezifit{\"a}t der PeB-Virus-Bindung wurde mittels geeigneter Kontrollen auf der Seite des Analyten und des Liganden nachgewiesen. Des Weiteren war das Peptid PeB in der Lage die Bindung von X31-Viren an Mimetika seines nat{\"u}rlichen Rezeptors zu inhibieren, was die spezifische Interaktion mit der Rezeptorbindungsstelle im H{\"a}magglutinin belegt. Anschließend wurde die Prim{\"a}rsequenz von PeB durch eine vollst{\"a}ndige Substitutionsanalyse im Microarray-Format hinsichtlich der Struktur-Aktivit{\"a}ts-Beziehungen charakterisiert. Dies f{\"u}hrte außerdem zu verbesserten Peptidvarianten mit erh{\"o}hter Affinit{\"a}t und breiterer Spezifit{\"a}t gegen aktuelle Influenzast{\"a}mme verschiedener Serotypen (z.B. H1N1/2009, H5N1/2004, H7N1/2013). Schließlich konnte durch Verwendung einer in der Prim{\"a}rsequenz angepassten h{\"o}her affinen Peptidvariante die Influenzainfektion in vitro inhibiert werden. Damit stellen die vom urspr{\"u}nglichen Peptid PeB abgeleiteten Varianten Rezeptormolek{\"u}le in biosensorischen Testsystemen sowie potentielle Wirkstoffe dar.},
  language  = {de}
}
@inproceedings{MemczakLausterHerrmannetal.2013,
  author    = {Memczak, Henry and Lauster, Daniel and Herrmann, Andreas and St{\"o}cklein, Walter F. M. and Bier, Frank Fabian},
  title     = {Novel hemagglutinin-binding peptides for biosensing and inhibition of Influenza Viruses},
  series = {Biopolymers},
  volume    = {100},
  booktitle = {Biopolymers},
  number    = {3},
  publisher = {Wiley-Blackwell},
  address   = {Hoboken},
  issn      = {0006-3525},
  pages     = {255 -- 255},
  year      = {2013},
  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}
}