@article{GhobadiHeuchelKratzetal.2014,
  author    = {Ghobadi, Ehsan and Heuchel, Matthias and Kratz, Karl and Lendlein, Andreas},
  title     = {Atomistic simulation of the shape-memory effect in dry and water swollen Poly[(rac-lactide)-co-glycolide] and copolyester urethanes thereof},
  series = {Macromolecular chemistry and physics},
  volume    = {215},
  journal   = {Macromolecular chemistry and physics},
  number    = {1},
  publisher = {Wiley-VCH},
  address   = {Weinheim},
  issn      = {1022-1352},
  doi       = {10.1002/macp.201300507},
  pages     = {65 -- 75},
  year      = {2014},
  abstract  = {An atomistic molecular dynamics simulation approach is applied to model the influence of urethane linker units as well as the addition of water molecules on the simulated shape-memory properties of poly[(rac-lactide)-co-glycolide] (PLGA) and PLGA-based copolyester urethanes comprising different urethane linkers. The shape-memory performance of these amorphous packing models is explored in a simulated heating-deformation-cooling-heating procedure. Depending on the type of incorporated urethane linker, the mechanical properties of the dry copolyester urethanes are found to be significantly improved compared with PLGA, which can be attributed to the number of intermolecular hydrogen bonds between the urethane units. Good shape-memory properties are observed for all the modeled systems. In the dry state, the shape fixation is found to be improved by implementation of urethane units. After swelling of the copolymer models with water, which results in a reduction of their glass transition temperatures, the relaxation kinetics during unloading and shape recovery are found to be substantially accelerated.},
  language  = {en}
}
@article{KunstmannEngstroemWehleetal.2020,
  author    = {Kunstmann, Ruth Sonja and Engstr{\"o}m, Olof and Wehle, Marko and Widmalm, G{\"o}ran and Santer, Mark and Barbirz, Stefanie},
  title     = {Increasing the affinity of an O-Antigen polysaccharide binding site in Shigella flexneri bacteriophage Sf6 tailspike protein},
  series = {Chemistry - A European Journal},
  volume    = {26},
  journal   = {Chemistry - A European Journal},
  number    = {32},
  publisher = {Wiley-VCH},
  address   = {Weinheim},
  issn      = {0947-6539},
  doi       = {10.1002/chem.202000495},
  pages     = {7263 -- 7273},
  year      = {2020},
  abstract  = {Broad and unspecific use of antibiotics accelerates spread of resistances. Sensitive and robust pathogen detection is thus important for a more targeted application. Bacteriophages contain a large repertoire of pathogen-binding proteins. These tailspike proteins (TSP) often bind surface glycans and represent a promising design platform for specific pathogen sensors. We analysed bacteriophage Sf6 TSP that recognizes the O-polysaccharide of dysentery-causing Shigella flexneri to develop variants with increased sensitivity for sensor applications. Ligand polyrhamnose backbone conformations were obtained from 2D H-1,H-1-trNOESY NMR utilizing methine-methine and methine-methyl correlations. They agreed well with conformations obtained from molecular dynamics (MD), validating the method for further predictions. In a set of mutants, MD predicted ligand flexibilities that were in good correlation with binding strength as confirmed on immobilized S. flexneri O-polysaccharide (PS) with surface plasmon resonance. In silico approaches combined with rapid screening on PS surfaces hence provide valuable strategies for TSP-based pathogen sensor design.},
  language  = {en}
}