@article{AdelsbergerKulkarniJainetal.2010,
  author    = {Adelsberger, Joseph and Kulkarni, Amit and Jain, Abhinav and Wang, Weinan and Bivigou Koumba, Achille Mayelle and Busch, Peter and Pipich, Vitaliy and Holderer, Olaf and Hellweg, Thomas and Laschewsky, Andr{\´e} and M{\"u}ller-Buschbaum, Peter and Papadakis, Christine M.},
  title     = {Thermoresponsive PS-b-PNIPAM-b-PS micelles : aggregation behavior, segmental dynamics, and thermal response},
  issn      = {0024-9297},
  doi       = {10.1021/Ma902714p},
  year      = {2010},
  abstract  = {We have studied I lie thermal behavior of amphiphilic, symmetric triblock copolymers having short, deuterated polystyrene (PS) end blocks and a large poly(N-isopropylacrylarnicle) (PNIPAM) middle block exhibiting a lower critical solution temperature (LCST) in aqueous solution. A wide range of concentrations (0.1-300 mg/mL) is investigated using it number of analytical methods such as fluorescence correlation spectroscopy (FCS), turbidimetry, dynamic light scattering (DLS), small-angle neutron scattering (SANS), and neutron spin-echo spectroscopy (NSE). The critical micelle concentration is determined using FCS to be 1 mu M or less. The collapse of the micelles at the LCST is investigated using turbidimetry and DLS and shows a weak dependence on the degree of polymerization of the PNIPAM block. SANS with contrast matching allows its to reveal the core-shell Structure of the micelles as well as their correlation as a function of temperature. The segmental dynamics of the PNIPAM shell are studied as a function of temperature and arc found to be faster in the collapsed state than in the swollen state. The mode detected has a linear dispersion in q(2) and is found to be faster in the collapsed state as compared to the swollen state. We attribute this result to the averaging over mobile and immobilized segments.},
  language  = {en}
}
@article{AdelsbergerMeierKollBivigouKoumbaetal.2011,
  author    = {Adelsberger, Joseph and Meier-Koll, Andreas and Bivigou Koumba, Achille Mayelle and Busch, Peter and Holderer, Olaf and Hellweg, Thomas and Laschewsky, Andr{\´e} and M{\"u}ller-Buschbaum, Peter and Papadakis, Christine M.},
  title     = {The collapse transition and the segmental dynamics in concentrated micellar solutions of P(S-b-NIPAM) diblock copolymers},
  series = {Colloid and polymer science : official journal of the Kolloid-Gesellschaft},
  volume    = {289},
  journal   = {Colloid and polymer science : official journal of the Kolloid-Gesellschaft},
  number    = {5-6},
  publisher = {Springer},
  address   = {New York},
  issn      = {0303-402X},
  doi       = {10.1007/s00396-011-2382-3},
  pages     = {711 -- 720},
  year      = {2011},
  abstract  = {We investigate concentrated solutions of poly(styrene-b-N-isopropyl acrylamide) (P(S-b-NIPAM)) diblock copolymers in deuterated water (D2O). Both structural changes and the changes of the segmental dynamics occurring upon heating through the lower critical solution temperature (LCST) of PNIPAM are studied using small-angle neutron scattering and neutron spin-echo spectroscopy. The collapse of the micellar shell and the cluster formation of collapsed micelles at the LCST as well as an increase of the segmental diffusion coefficient after crossing the LCST are detected. Comparing to our recent results on a triblock copolymer P(S-b-NIPAM-b-S) [25], we observe that the collapse transition of P(S-b-NIPAM) is more complex and that the PNIPAM segmental dynamics are faster than in P(S-b-NIPAM-b-S).},
  language  = {en}
}
@article{WellertTierschKoetzetal.2011,
  author    = {Wellert, Stefan and Tiersch, Brigitte and Koetz, Joachim and Richardt, Andre and Lapp, Alain and Holderer, Olaf and Gaeb, Juergen and Blum, Marc-Michael and Schulreich, Christoph and Stehle, Ralf and Hellweg, Thomas},
  title     = {The DFPase from Loligo vulgaris in sugar surfactant-based bicontinuous microemulsions structure, dynamics, and enzyme activity},
  series = {European biophysics journal : with biophysics letters ; an international journal of biophysics},
  volume    = {40},
  journal   = {European biophysics journal : with biophysics letters ; an international journal of biophysics},
  number    = {6},
  publisher = {Springer},
  address   = {New York},
  issn      = {0175-7571},
  doi       = {10.1007/s00249-011-0689-0},
  pages     = {761 -- 774},
  year      = {2011},
  abstract  = {The enzyme diisopropyl fluorophosphatase (DFPase) from the squid Loligo vulgaris is of great interest because of its ability to catalyze the hydrolysis of highly toxic organophosphates. In this work, the enzyme structure in solution (native state) was studied by use of different scattering methods. The results are compared with those from hydrodynamic model calculations based on the DFPase crystal structure. Bicontinuous microemulsions made of sugar surfactants are discussed as host systems for the DFPase. The microemulsion remains stable in the presence of the enzyme, which is shown by means of scattering experiments. Moreover, activity assays reveal that the DFPase still has high activity in this complex reaction medium. To complement the scattering experiments cryo-SEM was also employed to study the microemulsion structure.},
  language  = {en}
}