TY - JOUR A1 - Schöne, Anne-Christin A1 - Schulz, Burkhard A1 - Lendlein, Andreas T1 - Stimuli Responsive and Multifunctional Polymers: Progress in Materials and Applications JF - Macromolecular rapid communications Y1 - 2016 U6 - https://doi.org/10.1002/marc.201600650 SN - 1022-1336 SN - 1521-3927 VL - 37 SP - 1856 EP - 1859 PB - Wiley-VCH CY - Weinheim ER - TY - JOUR A1 - Schöne, Anne-Christin A1 - Kratz, Karl A1 - Schulz, Burkhard A1 - Lendlein, Andreas T1 - The relevance of hydrophobic segments in multiblock copolyesterurethanes for their enzymatic degradation at the air-water interface JF - Polymer : the international journal for the science and technology of polymers N2 - The interplay of an enzyme with a multiblock copolymer PDLCL containing two segments of different hydrophilicity and degradability is explored in thin films at the air-water interface. The enzymatic degradation was studied in homogenous Langmuir monolayers, which are formed when containing more than 40 wt% oligo(epsilon-caprolactone) (OCL). Enzymatic degradation rates were significantly reduced with increasing content of hydrophobic oligo(omega-pentadecalactone) (OPDL). The apparent deceleration of the enzymatic process is caused by smaller portion of water-soluble degradation fragments formed from degradable OCL fragments. Beside the film degradation, a second competing process occurs after adding lipase from Pseudomonas cepacia into the subphase, namely the enrichment of the lipase molecules in the polymeric monolayer. The incorporation of the lipase into the Langmuir film is experimentally revealed by concurrent surface area enlargement and by Brewster angle microscopy (BAM). Aside from the ability to provide information about the degradation behavior of polymers, the Langmuir monolayer degradation (LMD) approach enables to investigate polymer-enzyme interactions for non-degradable polymers. (C) 2016 Elsevier Ltd. All rights reserved. KW - Multiblock copolymer KW - Enzymatic polymer degradation KW - Oligo(omega-pentadecalactone) KW - Oligo(epsilon-caprolactone) KW - Langmuir monolayer degradation technique Y1 - 2016 U6 - https://doi.org/10.1016/j.polymer.2016.09.001 SN - 0032-3861 SN - 1873-2291 VL - 102 SP - 92 EP - 98 PB - Elsevier CY - Oxford ER - TY - JOUR A1 - Schöne, Anne-Christin A1 - Kratz, Karl A1 - Schulz, Burkhard A1 - Lendlein, Andreas T1 - Polymer architecture versus chemical structure as adjusting tools for the enzymatic degradation of oligo(epsilon-caprolactone) based films at the air-water interface JF - Polymer Degradation and Stability N2 - The enzymatic degradation of oligo(epsilon-caprolactone) (OCL) based films at the air-water interface is investigated by Langmuir monolayer degradation (LMD) experiments to elucidate the influence of the molecular architecture and of the chemical structure on the chain scission process. For that purpose, the interactions of 2D monolayers of two star-shaped poly(epsilon-caprolactone)s (PCLs) and three linear OCL based copolyesterurethanes (P(OCL-U)) with the lipase from Pseudomonas cepacia are evaluated in comparison to linear OCL. While the architecture of star-shaped PCL Langmuir layers slightly influences their degradability compared to OCL films, significantly retarded degradations are observed for P(OCL-U) films containing urethane junction units derived from 2, 2 (4), 4-trimethyl hexamethylene diisocyanate (TMDI), hexamethylene diisocyanate (HDI) or lysine ethyl ester diisocyanate (LDI). The enzymatic degradation of the OCL based 2D structures is related to the presence of hydrophilic groups within the macromolecules rather than to the packing density of the film or to the molecular weight. The results reveal that the LMD technique allows the parallel analysis of both the film/enzyme interactions and the degradation process on the molecular level. (C) 2016 Elsevier Ltd. All rights reserved. KW - Langmuir technique KW - Oligo(epsilon-caprolactone) KW - Enzymatic degradation KW - Polymer architecture Y1 - 2016 U6 - https://doi.org/10.1016/j.polymdegradstab.2016.07.010 SN - 0141-3910 SN - 1873-2321 VL - 131 SP - 114 EP - 121 PB - Elsevier CY - Oxford ER - TY - JOUR A1 - Machatschek, Rainhard Gabriel A1 - Schöne, Anne-Christin A1 - Raschdorf, Elisa A1 - Ihlenburg, Ramona A1 - Schulz, Burkhard A1 - Lendlein, Andreas T1 - Interfacial properties of morpholine-2,5-dione-based oligodepsipeptides and multiblock copolymers JF - MRS Communications N2 - Oligodepsipeptides (ODPs) with alternating amide and ester bonds prepared by ring-opening polymerization of morpholine-2,5-dione derivatives are promising matrices for drug delivery systems and building blocks for multifunctional biomaterials. Here, we elucidate the behavior of three telechelic ODPs and one multiblock copolymer containing ODP blocks at the air-water interface. Surprisingly, whereas the oligomers and multiblock copolymers crystallize in bulk, no crystallization is observed at the air-water interface. Furthermore, polarization modulation infrared reflection absorption spectroscopy is used to elucidate hydrogen bonding and secondary structures in ODP monolayers. The results will direct the development of the next ODP-based biomaterial generation with tailored properties for highly sophisticated applications. Y1 - 2019 U6 - https://doi.org/10.1557/mrc.2019.21 SN - 2159-6859 SN - 2159-6867 VL - 9 IS - 1 SP - 170 EP - 180 PB - Cambridge Univ. Press CY - New York ER -