@article{WischkeBaehrRachevaetal.2018,
  author    = {Wischke, Christian and Baehr, Elen and Racheva, Miroslava and Heuchel, Matthias and Weigel, Thomas and Lendlein, Andreas},
  title     = {Surface immobilization strategies for tyrosinase as biocatalyst applicable to polymer network synthesis},
  series = {MRS Advances},
  volume    = {3},
  journal   = {MRS Advances},
  number    = {63},
  publisher = {Cambridge Univ. Press},
  address   = {New York},
  issn      = {2059-8521},
  doi       = {10.1557/adv.2018.630},
  pages     = {3875 -- 3881},
  year      = {2018},
  abstract  = {Enzymes have recently attracted increasing attention in material research based on their capacity to catalyze the conversion of polymer-bound moieties for synthesizing polymer networks, particularly bulk hydrogels. hi this study. the surface immobilization of a relevant enzyme. mushroom tyrosinase, should be explored using glass as model surface. In a first step. the glass support was functionalized with silanes to introduce either amine or carboxyl groups, as confirmed e.g. by X-ray photoelectron spectroscopy. By applying glutaraldehyde and EDC/NHS chemistry, respectively, surfaces have been activated for subsequent successful coupling of tyrosinase. Via protein hydrolysis and amino acid characterization by HPLC, the quantity of bound tyrosinase was shown to correspond to a full surface coverage. Based on the visualized enzymatic conversion of a test substrate at the glass support. the functionalized surfaces may be explored for surface-associated material synthesis in the future.},
  language  = {en}
}
@article{TuncaboyluFriessWischkeetal.2018,
  author    = {Tuncaboylu, Deniz Ceylan and Friess, Fabian and Wischke, Christian and Lendlein, Andreas},
  title     = {A multifunctional multimaterial system for on-demand protein release},
  series = {Journal of controlled release},
  volume    = {284},
  journal   = {Journal of controlled release},
  publisher = {Elsevier},
  address   = {Amsterdam},
  issn      = {0168-3659},
  doi       = {10.1016/j.jconrel.2018.06.022},
  pages     = {240 -- 247},
  year      = {2018},
  abstract  = {In order to provide best control of the regeneration process for each individual patient, the release of protein drugs administered during surgery may need to be timely adapted and/or delayed according to the progress of healing/regeneration. This study aims to establish a multifunctional implant system for a local on-demand release, which is applicable for various types of proteins. It was hypothesized that a tubular multimaterial container kit, which hosts the protein of interest as a solution or gel formulation, would enable on-demand release if equipped with the capacity of diameter reduction upon external stimulation. Using devices from poly(epsilon-caprolactone) networks, it could be demonstrated that a shape-memory effect activated by heat or NIR light enabled on-demand tube shrinkage. The decrease of diameter of these shape-memory tubes (SMT) allowed expelling the payload as demonstrated for several proteins including SDF-1 alpha, a therapeutically relevant chemotactic protein, to achieve e.g. continuous release with a triggered add-on dosing (open tube) or an on-demand onset of bolus or sustained release (sealed tube). Considering the clinical relevance of protein factors in (stem) cell attraction to lesions and the progress in monitoring biomarkers in body fluids, such on-demand release systems may be further explored e.g. in heart, nerve, or bone regeneration in the future.},
  language  = {en}
}