@misc{BourgatTierschKoetzetal.2020,
  author    = {Bourgat, Yannick and Tiersch, Brigitte and Koetz, Joachim and Menzel, Henning},
  title     = {Enzyme degradable polymersomes from chitosan-g-[poly-l-lysine-block-epsilon-caprolactone] copolymer},
  series = {Zweitver{\"o}ffentlichungen der Universit{\"a}t Potsdam : Mathematisch-Naturwissenschaftliche Reihe},
  journal   = {Zweitver{\"o}ffentlichungen der Universit{\"a}t Potsdam : Mathematisch-Naturwissenschaftliche Reihe},
  number    = {1},
  issn      = {1866-8372},
  doi       = {10.25932/publishup-56658},
  url       = {http://nbn-resolving.de/urn:nbn:de:kobv:517-opus4-566584},
  pages     = {11},
  year      = {2020},
  abstract  = {The scope of this study includes the synthesis of chitosan-g-[peptide-poly-epsilon-caprolactone] and its self-assembly into polymeric vesicles employing the solvent shift method. In this way, well-defined core-shell structures suitable for encapsulation of drugs are generated. The hydrophobic polycaprolactone side-chain and the hydrophilic chitosan backbone are linked via an enzyme-cleavable peptide. The synthetic route involves the functionalization of chitosan with maleimide groups and the preparation of polycaprolactone with alkyne end-groups. A peptide functionalized with a thiol group on one side and an azide group on the other side is prepared. Thiol-ene click-chemistry and azide-alkyne Huisgen cycloaddition are then used to link the chitosan and poly-epsilon-caprolactone chains, respectively, with this peptide. For a preliminary study, poly-l-lysin is a readily available and cleavable peptide that is introduced to investigate the feasibility of the system. The size and shape of the polymersomes are studied by dynamic light scattering and cryo-scanning electron microscopy. Furthermore, degradability is studied by incubating the polymersomes with two enzymes, trypsin and chitosanase. A dispersion of polymersomes is used to coat titanium plates and to further test the stability against enzymatic degradation.},
  language  = {en}
}
@article{BourgatTierschKoetzetal.2020,
  author    = {Bourgat, Yannick and Tiersch, Brigitte and Koetz, Joachim and Menzel, Henning},
  title     = {Enzyme degradable polymersomes from chitosan-g-[poly-l-lysine-block-epsilon-caprolactone] copolymer},
  series = {Macromolecular bioscience},
  volume    = {21},
  journal   = {Macromolecular bioscience},
  number    = {1},
  publisher = {Wiley-VCH},
  address   = {Weinheim},
  issn      = {1616-5187},
  doi       = {10.1002/mabi.202000259},
  pages     = {1 -- 9},
  year      = {2020},
  abstract  = {The scope of this study includes the synthesis of chitosan-g-[peptide-poly-epsilon-caprolactone] and its self-assembly into polymeric vesicles employing the solvent shift method. In this way, well-defined core-shell structures suitable for encapsulation of drugs are generated. The hydrophobic polycaprolactone side-chain and the hydrophilic chitosan backbone are linked via an enzyme-cleavable peptide. The synthetic route involves the functionalization of chitosan with maleimide groups and the preparation of polycaprolactone with alkyne end-groups. A peptide functionalized with a thiol group on one side and an azide group on the other side is prepared. Thiol-ene click-chemistry and azide-alkyne Huisgen cycloaddition are then used to link the chitosan and poly-epsilon-caprolactone chains, respectively, with this peptide. For a preliminary study, poly-l-lysin is a readily available and cleavable peptide that is introduced to investigate the feasibility of the system. The size and shape of the polymersomes are studied by dynamic light scattering and cryo-scanning electron microscopy. Furthermore, degradability is studied by incubating the polymersomes with two enzymes, trypsin and chitosanase. A dispersion of polymersomes is used to coat titanium plates and to further test the stability against enzymatic degradation.},
  language  = {en}
}