@article{BogomolovaSeckerKoetzetal.2017,
  author    = {Bogomolova, Anna and Secker, Christian and Koetz, Joachim and Schlaad, Helmut},
  title     = {Thermo-induced multistep assembly of double-hydrophilic block copolypeptoids in water},
  series = {Colloid and polymer science : official journal of the Kolloid-Gesellschaft},
  volume    = {295},
  journal   = {Colloid and polymer science : official journal of the Kolloid-Gesellschaft},
  publisher = {Springer},
  address   = {New York},
  issn      = {0303-402X},
  doi       = {10.1007/s00396-017-4044-6},
  pages     = {1305 -- 1312},
  year      = {2017},
  abstract  = {The aqueous solution behavior of thermoresponsive-hydrophilic block copolypeptoids, i.e., poly(N-(n-propyl)glycine) (x) -block-poly(N-methylglycine) (y) (x = 70; y = 23, 42, 76), in the temperature range of 20-45 A degrees C is studied. Turbidimetric analyses of the 0.1 wt\% aqueous solutions reveal two cloud points at T (cp)similar to 30 and 45 A degrees C and a clearing point in between at T (cl)similar to 42 A degrees C. Temperature-dependent dynamic light scattering (DLS) suggest that right above the first collapse temperature, single polymer molecules assemble into large structures which upon further heating, i.e., at the clearing point temperature, disassemble into micelle-like structures. Upon further heating, the aggregates start to grow again in size, as recognized by the second cloud point, through a crystallization process.},
  language  = {en}
}
@article{RichterSchulzSubkowskietal.2016,
  author    = {Richter, Marina Juliane and Schulz, Alexander and Subkowski, Thomas and B{\"o}ker, Alexander},
  title     = {Adsorption and rheological behavior of an amphiphilic protein at oil/water interfaces},
  series = {Journal of colloid and interface science},
  volume    = {479},
  journal   = {Journal of colloid and interface science},
  publisher = {Elsevier},
  address   = {San Diego},
  issn      = {0021-9797},
  doi       = {10.1016/j.jcis.2016.06.062},
  pages     = {199 -- 206},
  year      = {2016},
  abstract  = {Hydrophobins are highly surface active proteins which self-assemble at hydrophilic-hydrophobic interfaces into amphipathic membranes. We investigate hydrophobin self-assembly at oil/water interfaces to deepen the understanding of protein behavior in order to improve our biomimetic synthesis. Therefore, we carried out pendant drop measurements of hydrophobin stabilized oil/water systems determining the time-dependent IFT and the dilatational rheology with additional adaptation to the Serrien protein model. We show that the class I hydrophobin H*Protein B adsorbs at an oil/water interface where it forms a densely-packed interfacial protein layer, which dissipates energy during droplet oscillation. Furthermore, the interfacial protein layer exhibits shear thinning behavior. (C) 2016 Elsevier Inc. All rights reserved.},
  language  = {en}
}