TY - GEN A1 - Wessig, Pablo A1 - Bader, Denise A1 - Klier, Dennis Tobias A1 - Hettrich, Cornelia A1 - Bier, Frank Fabian T1 - Detecting carbohydrate–lectin interactions using a fluorescent probe based on DBD dyes N2 - 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. T3 - Zweitveröffentlichungen der Universität Potsdam : Mathematisch-Naturwissenschaftliche Reihe - 314 KW - conformational-changes KW - green-i KW - protein KW - binding KW - assay Y1 - 2016 U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:kobv:517-opus4-394382 SP - 1235 EP - 1238 ER - TY - JOUR A1 - Pavashe, Prashant A1 - Elamparuthi, Elangovan A1 - Hettrich, Cornelia A1 - Moeller, Heiko M. A1 - Linker, Torsten T1 - Synthesis of 2-Thiocarbohydrates and Their Binding to Concanavalin A JF - The journal of organic chemistry N2 - A convenient and general synthesis of 2-thiocarbohydrates via cerium ammonium nitrate oxidation of the thiocyanate ion is described. Radical addition to glycals proceeds with excellent regio- and good stereoselectivities in only one step, deprotection affords water-soluble 2-thio saccharides. Binding studies to Con A have been performed by isothermal titration calorimetry (ITC) and saturation transfer difference (STD) NMR spectroscopy. The 2-thiomannose derivative binds even stronger to Con A than the natural substrate, offering opportunities for new lectin or enzyme inhibitors. Y1 - 2016 U6 - https://doi.org/10.1021/acs.joc.6b00987 SN - 0022-3263 VL - 81 SP - 8595 EP - 8603 PB - American Chemical Society CY - Washington ER - TY - JOUR A1 - Hüttl, Christine A1 - Hettrich, Cornelia A1 - Riedel, Melanie A1 - Henklein, Petra A1 - Rawel, Harshadrai Manilal A1 - Bier, Frank Fabian T1 - Development of Peptidyl Lysine Dendrons: 1,3-Dipolar Cycloaddition for Peptide Coupling and Antibody Recognition JF - Chemical biology & drug design N2 - A straightforward synthesis strategy to multimerize a peptide mimotopes for antibody B13-DE1 recognition is described based on lysine dendrons as multivalent scaffolds. Lysine dendrons that possess N-terminal alkyne residues at the periphery were quantitative functionalized with azido peptides using click chemistry. The solid-phase peptide synthesis (SPPS) allows preparing the peptide dendron in high purity and establishing the possibility of automation. The presented peptide dendron is a promising candidate as multivalent ligand and was used for antibody B13-DE1 recognition. The binding affinity increases with higher dendron generation without loss of specificity. The analysis of biospecific interaction between the synthesized peptide dendron and the antibody was done via surface plasmon resonance (SPR) technique. The presented results show a promising tool for investigations of antigen-antibody reactions. KW - click chemistry KW - lysine dendron KW - peptide mimotopes KW - solid-phase peptide synthesis KW - surface plasmon resonance Y1 - 2015 U6 - https://doi.org/10.1111/cbdd.12444 SN - 1747-0277 SN - 1747-0285 VL - 85 IS - 5 SP - 565 EP - 573 PB - Wiley-Blackwell CY - Hoboken ER - TY - JOUR A1 - Hüttl, Christine A1 - Hettrich, Cornelia A1 - Miller, Reinhard A1 - Paulke, Bernd-Reiner A1 - Henklein, Petra A1 - Rawel, Harshadrai Manilal A1 - Bier, Frank Fabian T1 - Self-assembled peptide amphiphiles function as multivalent binder with increased hemagglutinin affinity JF - BMC biotechnology N2 - Background: A promising way in diagnostic and therapeutic applications is the development of peptide amphiphiles (PAs). Peptides with a palmitic acid alkylchain were designed and characterized to study the effect of the structure modifications on self-assembling capabilities and the multiple binding capacity to hemagglutinin (HA), the surface protein of influenza virus type A. The peptide amphiphiles consists of a hydrophilic headgroup with a biological functionality of the peptide sequence and a chemically conjugated hydrophobic tail. In solution they self-assemble easily to micelles with a hydrophobic core surrounded by a closely packed peptide-shell. Results: In this study the effect of a multiple peptide binding partner to the receptor binding site of HA could be determined with surface plasmon resonance measurements. The applied modification of the peptides causes signal amplification in relationship to the unmodified peptide wherein the high constant specificity persists. The molecular assembly of the peptides was characterized by the determination of critical micelle concentration (CMC) with concentration of 10(-5) M and the colloidal size distribution. Conclusion: The modification of the physico-chemical parameters by producing peptide amphiphiles form monomeric structures which enhances the binding affinity and allows a better examination of the interaction with the virus surface protein hemagglutinin. KW - CMC KW - Influenza virus detection KW - Micelle KW - PAs KW - Surface plasmon resonance Y1 - 2013 U6 - https://doi.org/10.1186/1472-6750-13-51 SN - 1472-6750 VL - 13 IS - 22 PB - BioMed Central CY - London ER - TY - JOUR A1 - Couturier, Jean-Philippe A1 - Wischerhoff, Erik A1 - Bernin, Robert A1 - Hettrich, Cornelia A1 - Koetz, Joachim A1 - Sutterlin, Martin A1 - Tiersch, Brigitte A1 - Laschewsky, Andre T1 - Thermoresponsive Polymers and Inverse Opal Hydrogels for the Detection of Diols JF - Langmuir N2 - Responsive inverse opal hydrogels functionalized by boroxole moieties were synthesized and explored as sensor platforms for various low molar mass as well as polymeric diols and polyols, including saccharides, glycopolymers and catechols, by exploiting the diol induced modulation of their structural color. The underlying thermoresponsive water-soluble copolymers and hydrogels exhibit a coil-to-globule or volume phase transition, respectively, of the LCST-type. They were prepared from oligoethylene oxide methacrylate (macro)monomers and functionalized via copolymerization to bear benzoboroxole moieties. The resulting copolymers represent weak polyacids, which can bind specifically to diols within an appropriate pH window. Due to the resulting modulation of the overall hydrophilicity of the systems and the consequent shift of their phase transition temperature, the usefulness of such systems for indicating the presence of catechols, saccharides, and glycopolymers was studied, exploiting the diol/polyol induced shifts of the soluble polymers’ cloud point, or the induced changes of the hydrogels’ swelling. In particular, the increased acidity of benzoboroxoles compared to standard phenylboronic acids allowed performing the studies in PBS buffer (phosphate buffered saline) at the physiologically relevant pH of 7.4. The inverse opals constructed of these thermo- and analyte-responsive hydrogels enabled following the binding of specific diols by the induced shift of the optical stop band. Their highly porous structure enabled the facile and specific optical detection of not only low molar mass but also of high molar mass diol/polyol analytes such as glycopolymers. Accordingly, such thermoresponsive inverse opal systems functionalized with recognition units represent attractive and promising platforms for the facile sensing of even rather big analytes by simple optical means, or even by the bare eye. Y1 - 2016 U6 - https://doi.org/10.1021/acs.langmuir.6b00803 SN - 0743-7463 VL - 32 SP - 4333 EP - 4345 PB - American Chemical Society CY - Washington ER - TY - JOUR A1 - Couturier, Jean-Philippe A1 - Sütterlin, Martin A1 - Laschewsky, André A1 - Hettrich, Cornelia A1 - Wischerhoff, Erik T1 - Responsive Inverse Opal Hydrogels for the Sensing of Macromolecules JF - Angewandte Chemie : a journal of the Gesellschaft Deutscher Chemiker ; International edition N2 - Dual responsive inverse opal hydrogels were designed as autonomous sensor systems for (bio)macromolecules, exploiting the analyte-induced modulation of the opal's structural color. The systems that are based on oligo(ethylene glycol) macromonomers additionally incorporate comonomers with various recognition units. They combine a coil-to-globule collapse transition of the LCST type with sensitivity of the transition temperature toward molecular recognition processes. This enables the specific detection of macromolecular analytes, such as glycopolymers and proteins, by simple optical methods. While the inverse opal structure assists the effective diffusion even of large analytes into the photonic crystal, the stimulus responsiveness gives rise to strong shifts of the optical Bragg peak of more than 100nm upon analyte binding at a given temperature. The systems' design provides a versatile platform for the development of easy-to-use, fast, and low-cost sensors for pathogens. KW - hydrogels KW - photonic crystals KW - polymers KW - responsive materials KW - sensors Y1 - 2015 U6 - https://doi.org/10.1002/anie.201500674 SN - 1433-7851 SN - 1521-3773 VL - 54 IS - 22 SP - 6641 EP - 6644 PB - Wiley-VCH CY - Weinheim ER -