@article{TeixeiraBlanzatKoetzetal.2006, author = {Teixeira, C. V. and Blanzat, Muriel and Koetz, Joachim and Rico-Lattes, I. and Brezesinski, Gerald}, title = {In-plane miscibility and mixed bilayer microstructure in mixtures of catanionic glycolipids and zwitterionic phospholipids}, series = {Biochimica et biophysica acta : Biomembranes}, volume = {1758}, journal = {Biochimica et biophysica acta : Biomembranes}, publisher = {Elsevier}, address = {Amsterdam}, issn = {0005-2736}, doi = {10.1016/j.bbamem.2006.05.025}, pages = {1797 -- 1808}, year = {2006}, abstract = {SAXS/WAXS studies were performed in combination with freeze fracture electron microscopy using mixtures of a new Gemini catanionic surfactant (Gem 16-12, formed by two sugar groups bound by a hydrocarbon spacer with 12 carbons and two 16-carbon chains) and the zwitterionic phospholipid 1,2-dipalmitoyl-sn-glycero-3-phosphocholine(DPPC) to establish the phase diagram. Gem 16-12 in water forms bilayers with the same amount of hydration water as DPPC. A frozen interdigitated phase with a low hydration number is observed below room temperature. The kinetics of the formation of this crystalline phase is very slow. Above the chain melting temperature, multilayered vesicles are formed. Mixing with DPPC produces mixed bilayers above the corresponding chain melting temperature. At room temperature, partially lamellar aggregates with local nematic order are observed. Splitting of infinite lamellae into discs is linked to immiscibility in frozen state. The ordering process is always accompanied by dehydration of the system. As a consequence, an unusual order-disorder phase transition upon cooling is observed.}, 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} }