@article{HundertmarkDimovaLengefeldetal.2011, author = {Hundertmark, Michaela and Dimova, Rumiana and Lengefeld, Jan and Seckler, Robert and Hincha, Dirk K.}, title = {The intrinsically disordered late embryogenesis abundant protein LEA18 from Arabidopsis thaliana modulates membrane stability through binding and folding.}, issn = {0006-3002}, year = {2011}, abstract = {Intrinsically disordered proteins (IDPs) constitute a substantial part of cellular proteomes. Late embryogenesis abundant (LEA) proteins are mostly predicted to be IDPs associated with dehydration tolerance in many plant, animal and bacterial species. Their functions, however, are largely unexplored and also their structure and interactions with potential target molecules have only recently been experimentally investigated in a small number of proteins. Here, we report on the structure and interactions with membranes of the Pfam LEA_1 protein LEA18 from the higher plant Arabidopsis thaliana. This functionally uncharacterized positively charged protein specifically aggregated and destabilized negatively charged liposomes. Isothermal titration calorimetry showed binding of the protein to both charged and uncharged membranes. LEA18 alone was largely unstructured in solution. While uncharged membranes had no influence on the secondary structure of LEA18, the protein partially folded into ;-sheet structure in the presence of negatively charged liposomes. These data suggest that LEA18 does not function as a membrane stabilizing protein, as suggested for other LEA proteins. Instead, a possible function of LEA18 could be the composition-dependent modulation of membrane stability, e.g., during signaling or vesicle-mediated transport. Research Highlights}, language = {en} } @article{HundertmarkDimovaLengefeldetal.2011, author = {Hundertmark, Michaela and Dimova, Rumiana and Lengefeld, Jan and Seckler, Robert and Hincha, Dirk K.}, title = {The intrinsically disordered late embryogenesis abundant protein LEA18 from Arabidopsis thaliana modulates membrane stability through binding and folding}, series = {Biochimica et biophysica acta : Biomembranes}, volume = {1808}, journal = {Biochimica et biophysica acta : Biomembranes}, number = {1}, publisher = {Elsevier}, address = {Amsterdam}, issn = {0005-2736}, doi = {10.1016/j.bbamem.2010.09.010}, pages = {446 -- 453}, year = {2011}, abstract = {Intrinsically disordered proteins (IDPs) constitute a substantial part of cellular proteomes. late embryogenesis abundant (LEA) proteins are mostly predicted to be IDPs associated with dehydration tolerance in many plant, animal and bacterial species. Their functions, however, are largely unexplored and also their structure and interactions with potential target molecules have only recently been experimentally investigated in a small number of proteins. Here, we report on the structure and interactions with membranes of the Pfam LEA_1 protein LEA18 from the higher plant Arabidopsis thaliana. This functionally uncharacterized positively charged protein specifically aggregated and destabilized negatively charged liposomes. Isothermal titration calorimetry showed binding of the protein to both charged and uncharged membranes. LEA18 alone was largely unstructured in solution. While uncharged membranes had no influence on the secondary structure of LEA18, the protein partially folded into beta-sheet structure in the presence of negatively charged liposomes. These data suggest that LEA18 does not function as a membrane stabilizing protein, as suggested for other LEA proteins. Instead, a possible function of LEA18 could be the composition-dependent modulation of membrane stability, e.g., during signaling or vesicle-mediated transport.}, language = {en} } @article{CasseShkilnyyLindersetal.2012, author = {Casse, Olivier and Shkilnyy, Andriy and Linders, J{\"u}rgen and Mayer, Christian and H{\"a}ussinger, Daniel and V{\"o}lkel, Antje and Th{\"u}nemann, Andreas F. and Dimova, Rumiana and C{\"o}lfen, Helmut and Meier, Wolfgang P. and Schlaad, Helmut and Taubert, Andreas}, title = {Solution behavior of double-hydrophilic block copolymers in dilute aqueous solution}, series = {Macromolecules : a publication of the American Chemical Society}, volume = {45}, journal = {Macromolecules : a publication of the American Chemical Society}, number = {11}, publisher = {American Chemical Society}, address = {Washington}, issn = {0024-9297}, doi = {10.1021/ma300621g}, pages = {4772 -- 4777}, year = {2012}, abstract = {The self-assembly of double-hydrophilic poly(ethylene oxide)-poly(2-methyl-2-oxazoline) diblock copolymers in water has been studied. Isothermal titration calorimetry, small-angle X-ray scattering, and analytical ultracentrifugation suggest that only single polymer chains are present in solution. In contrast, light scattering and transmission electron microscopy detect aggregates with radii of ca. 100 nm. Pulsed field gradient NMR spectroscopy confirms the presence of aggregates, although only 2\% of the polymer chains undergo aggregation. Water uptake experiments indicate differences in the hydrophilicity of the two blocks, which is believed to be the origin of the unexpected aggregation behavior (in accordance with an earlier study by Ke et al. [Macromolecules 2009, 42, 5339-5344]). The data therefore suggest that even in double-hydrophilic block copolymers, differences in hydrophilicity are sufficient to drive polymer aggregation, a phenomenon that has largely been overlooked or ignored so far.}, language = {en} } @phdthesis{Dimova2011, author = {Dimova, Rumiana}, title = {Probing the membrane nanoregime with optical microscopy}, address = {Potsdam}, pages = {50 S.}, year = {2011}, language = {en} } @inproceedings{RamadanGuerreroNedielkovetal.2021, author = {Ramadan, Shahenda and Guerrero, Paula and Nedielkov, Ruslan and Klishin, Nikolai and Dimova, Rumiana and Silva, Daniel V. and M{\"o}ller, Heiko}, title = {Building a mimetic system for unraveling protein-protein interactions on membranes}, series = {European biophysics journal : with biophysics letters ; an international journal of biophysics}, volume = {50}, booktitle = {European biophysics journal : with biophysics letters ; an international journal of biophysics}, number = {SUPPL 1}, publisher = {Springer}, address = {Berlin ; Heidelberg ; New York}, issn = {0175-7571}, doi = {10.1007/s00249-021-01558-w}, pages = {S153 -- S153}, year = {2021}, language = {en} } @inproceedings{StephanBarbirzRobinsonetal.2021, author = {Stephan, Mareike Sophia and Barbirz, Stefanie and Robinson, Tom and Yandrapalli, Naresh and Dimova, Rumiana}, title = {Bacterial mimetic systems for studying bacterial inactivation and infection}, series = {Biophysical journal : BJ / ed. by the Biophysical Society}, volume = {120}, booktitle = {Biophysical journal : BJ / ed. by the Biophysical Society}, number = {3}, publisher = {Cell Press}, address = {Cambridge}, issn = {0006-3495}, doi = {10.1016/j.bpj.2020.11.1087}, pages = {148A -- 148A}, year = {2021}, language = {en} } @article{GeorgievGrafmuellerBlegeretal.2018, author = {Georgiev, Vasil N. and Grafm{\"u}ller, Andrea and Bl{\´e}ger, David and Hecht, Stefan and Kunstmann, Sonja and Barbirz, Stefanie and Lipowsky, Reinhard and Dimova, Rumiana}, title = {Area increase and budding in giant vesicles triggered by light}, series = {Advanced science}, volume = {5}, journal = {Advanced science}, number = {8}, publisher = {Wiley}, address = {Hoboken}, issn = {2198-3844}, doi = {10.1002/advs.201800432}, pages = {9}, year = {2018}, abstract = {Biomembranes are constantly remodeled and in cells, these processes are controlled and modulated by an assortment of membrane proteins. Here, it is shown that such remodeling can also be induced by photoresponsive molecules. The morphological control of giant vesicles in the presence of a water-soluble ortho-tetrafluoroazobenzene photoswitch (F-azo) is demonstrated and it is shown that the shape transformations are based on an increase in membrane area and generation of spontaneous curvature. The vesicles exhibit budding and the buds can be retracted by using light of a different wavelength. In the presence of F-azo, the membrane area can increase by more than 5\% as assessed from vesicle electrodeformation. To elucidate the underlying molecular mechanism and the partitioning of F-azo in the membrane, molecular dynamics simulations are employed. Comparison with theoretically calculated shapes reveals that the budded shapes are governed by curvature elasticity, that the spontaneous curvature can be decomposed into a local and a nonlocal contribution, and that the local spontaneous curvature is about 1/(2.5 mu m). The results show that exo- and endocytotic events can be controlled by light and that these photoinduced processes provide an attractive method to change membrane area and morphology.}, language = {en} } @misc{GeorgievGrafmuellerBlegeretal.2018, author = {Georgiev, Vasil N. and Grafm{\"u}ller, Andrea and Bl{\´e}ger, David and Hecht, Stefan and Kunstmann, Ruth Sonja and Barbirz, Stefanie and Lipowsky, Reinhard and Dimova, Rumiana}, title = {Area increase and budding in giant vesicles triggered by light}, series = {Postprints der Universit{\"a}t Potsdam : Mathematisch-Naturwissenschaftliche Reihe}, volume = {5}, journal = {Postprints der Universit{\"a}t Potsdam : Mathematisch-Naturwissenschaftliche Reihe}, number = {733}, issn = {1866-8372}, doi = {10.25932/publishup-42629}, url = {http://nbn-resolving.de/urn:nbn:de:kobv:517-opus4-426298}, pages = {9}, year = {2018}, abstract = {Biomembranes are constantly remodeled and in cells, these processes are controlled and modulated by an assortment of membrane proteins. Here, it is shown that such remodeling can also be induced by photoresponsive molecules. The morphological control of giant vesicles in the presence of a water-soluble ortho-tetrafluoroazobenzene photoswitch (F-azo) is demonstrated and it is shown that the shape transformations are based on an increase in membrane area and generation of spontaneous curvature. The vesicles exhibit budding and the buds can be retracted by using light of a different wavelength. In the presence of F-azo, the membrane area can increase by more than 5\% as assessed from vesicle electrodeformation. To elucidate the underlying molecular mechanism and the partitioning of F-azo in the membrane, molecular dynamics simulations are employed. Comparison with theoretically calculated shapes reveals that the budded shapes are governed by curvature elasticity, that the spontaneous curvature can be decomposed into a local and a nonlocal contribution, and that the local spontaneous curvature is about 1/(2.5 mu m). The results show that exo- and endocytotic events can be controlled by light and that these photoinduced processes provide an attractive method to change membrane area and morphology.}, language = {en} }