@article{RosencrantzVuHoaNguyenParketal.2016, author = {Rosencrantz, Ruben R. and Vu Hoa Nguyen, and Park, Hyunji and Schulte, Christine and B{\"o}ker, Alexander and Schnakenberg, Uwe and Elling, Lothar}, title = {Lectin binding studies on a glycopolymer brush flow-through biosensor by localized surface plasmon resonance}, series = {Analytical and bioanalytical chemistry : a merger of Fresenius' journal of analytical chemistry and Analusis}, volume = {408}, journal = {Analytical and bioanalytical chemistry : a merger of Fresenius' journal of analytical chemistry and Analusis}, publisher = {Springer}, address = {Heidelberg}, issn = {1618-2642}, doi = {10.1007/s00216-016-9667-9}, pages = {5633 -- 5640}, year = {2016}, abstract = {A localized surface plasmon resonance biosensor in a flow-through configuration was applied for investigating kinetics of lectin binding to surface-grafted glycopolymer brushes. Polycarbonate filter membranes with pore sizes of 400 nm were coated with a 114-nm thick gold layer and used as substrate for surface-initiated atom-transfer radical polymerization of a glycomonomer. These grafted from glycopolymer brushes were further modified with two subsequent enzymatic reactions on the surface to yield an immobilized trisaccharide presenting brush. Specific binding of lectins including Clostridium difficile toxin A receptor domain to the glycopolymer brush surface could be investigated in a microfluidic setup with flow-through of the analytes and transmission surface plasmon resonance spectroscopy.}, language = {en} } @article{ReinickeReesEspeeletal.2017, author = {Reinicke, Stefan and Rees, Huw C. and Espeel, Pieter and Vanparijs, Nane and Bisterfeld, Carolin and Dick, Markus and Rosencrantz, Ruben R. and Brezesinski, Gerald and de Geest, Bruno G. and Du Prez, Filip E. and Pietruszka, J{\"o}rg and B{\"o}ker, Alexander}, title = {Immobilization of 2-Deoxy-D-ribose-5-phosphate Aldolase in Polymeric Thin Films via the Langmuir-Schaefer Technique}, series = {ACS applied materials \& interfaces}, volume = {9}, journal = {ACS applied materials \& interfaces}, publisher = {American Chemical Society}, address = {Washington}, issn = {1944-8244}, doi = {10.1021/acsami.6b13632}, pages = {8317 -- 8326}, year = {2017}, abstract = {A synthetic protocol for the fabrication of ultrathin polymeric films containing the enzyme 2-deoxy-D-ribose-5-phosphate aldolase from Escherichia coli (DERA(EC)) is presented. Ultrathin enzymatically active films are useful for applications in which only small quantities of active material are needed and at the same time quick response and contact times without diffusion limitation are wanted. We show how DERA as an exemplary enzyme can be immobilized in a thin polymer layer at the air-water interface and transferred to a suitable support by the Langmuir-Schaefer technique under full conservation of enzymatic activity. The polymer in use is a poly(N-isopropylacrylamide-co-N-2-thiolactone acrylamide) (P(NIPAAm-co-TlaAm)) statistical copolymer in which the thiolactone units serve a multitude of purposes including hydrophobization of the polymer, covalent binding of the enzyme and the support and finally cross-linking of the polymer matrix. The application of this type of polymer keeps the whole approach simple as additional cocomponents such as cross-linkers are avoided.}, language = {en} } @article{QiuZhangBicketal.2021, author = {Qiu, Liang and Zhang, Haoran and Bick, Thomas and Martin, Johannes and Wendler, Petra and B{\"o}ker, Alexander and Glebe, Ulrich and Xing, Chengfen}, title = {Construction of highly ordered glyco-inside nano-assemblies through RAFT dispersion polymerization of galactose-decorated monomer}, series = {Angewandte Chemie : a journal of the Gesellschaft Deutscher Chemiker ; International edition}, volume = {60}, journal = {Angewandte Chemie : a journal of the Gesellschaft Deutscher Chemiker ; International edition}, number = {20}, publisher = {Wiley-VCH}, address = {Weinheim}, issn = {1433-7851}, doi = {10.1002/anie.202015692}, pages = {11098 -- 11103}, year = {2021}, abstract = {Glyco-assemblies derived from amphiphilic sugar-decorated block copolymers (ASBCs) have emerged prominently due to their wide application, for example, in biomedicine and as drug carriers. However, to efficiently construct these glyco-assemblies is still a challenge. Herein, we report an efficient technology for the synthesis of glyco-inside nano-assemblies by utilizing RAFT polymerization of a galactose-decorated methacrylate for polymerization-induced self-assembly (PISA). Using this approach, a series of highly ordered glyco-inside nano-assemblies containing intermediate morphologies were fabricated by adjusting the length of the hydrophobic glycoblock and the polymerization solids content. A specific morphology of complex vesicles was captured during the PISA process and the formation mechanism is explained by the morphology of its precursor and intermediate. Thus, this method establishes a powerful route to fabricate glyco-assemblies with tunable morphologies and variable sizes, which is significant to enable the large-scale fabrication and wide application of glyco-assemblies.}, language = {en} } @article{RuebsamStompsBoekeretal.2017, author = {R{\"u}bsam, Kristin and Stomps, Benjamin Ren{\´e} Harald and B{\"o}ker, Alexander and Jakob, Felix and Schwaneberg, Ulrich}, title = {Anchor peptides: A green and versatile method for polypropylene functionalization}, series = {Polymer : the international journal for the science and technology of polymers}, volume = {116}, journal = {Polymer : the international journal for the science and technology of polymers}, publisher = {Elsevier}, address = {Oxford}, issn = {0032-3861}, doi = {10.1016/j.polymer.2017.03.070}, pages = {124 -- 132}, year = {2017}, language = {en} } @article{ZhangBramskiTutusetal.2019, author = {Zhang, Shuhao and Bramski, Julia and Tutus, Murat and Pietruszka, J{\"o}rg and B{\"o}ker, Alexander and Reinicke, Stefan}, title = {A Biocatalytically Active Membrane Obtained from Immobilization of 2-Deoxy-D-ribose-5-phosphate Aldolase on a Porous Support}, series = {ACS applied materials \& interfaces}, volume = {11}, journal = {ACS applied materials \& interfaces}, number = {37}, publisher = {American Chemical Society}, address = {Washington}, issn = {1944-8244}, doi = {10.1021/acsami.9b12029}, pages = {34441 -- 34453}, year = {2019}, abstract = {Aldol reactions play an important role in organic synthesis, as they belong to the class of highly beneficial C-C-linking reactions. Aldol-type reactions can be efficiently and stereoselectively catalyzed by the enzyme 2-deoxy-D-ribose-5-phosphate aldolase (DERA) to gain key intermediates for pharmaceuticals such as atorvastatin. The immobilization of DERA would open the opportunity for a continuous operation mode which gives access to an efficient, large-scale production of respective organic intermediates. In this contribution, we synthesize and utilize DERA/polymer conjugates for the generation and fixation of a DERA bearing thin film on a polymeric membrane support. The conjugation strongly increases the tolerance of the enzyme toward the industrial relevant substrate acetaldehyde while UV-cross-linkable groups along the conjugated polymer chains provide the opportunity for covalent binding to the support. First, we provide a thorough characterization of the conjugates followed by immobilization tests on representative, nonporous cycloolefinic copolymer supports. Finally, immobilization on the target supports constituted of polyacrylonitrile (PAN) membranes is performed, and the resulting enzymatically active membranes are implemented in a simple membrane module setup for the first assessment of biocatalytic performance in the continuous operation mode using the combination hexanal/acetaldehyde as the substrate.}, language = {en} }