@article{FedericoPiercePilusoetal.2015,
  author    = {Federico, Stefania and Pierce, Benjamin F. and Piluso, Susanna and Wischke, Christian and Lendlein, Andreas and Neffe, Axel T.},
  title     = {Design of Decorin-Based Peptides That Bind to CollagenI and their Potential as Adhesion Moieties in Biomaterials},
  series = {Angewandte Chemie : a journal of the Gesellschaft Deutscher Chemiker ; International edition},
  volume    = {54},
  journal   = {Angewandte Chemie : a journal of the Gesellschaft Deutscher Chemiker ; International edition},
  number    = {37},
  publisher = {Wiley-VCH},
  address   = {Weinheim},
  issn      = {1433-7851},
  doi       = {10.1002/anie.201505227},
  pages     = {10980 -- 10984},
  year      = {2015},
  abstract  = {Mimicking the binding epitopes of protein-protein interactions by using small peptides is important for generating modular biomimetic systems. A strategy is described for the design of such bioactive peptides without accessible structural data for the targeted interaction, and the effect of incorporating such adhesion peptides in complex biomaterial systems is demonstrated. The highly repetitive structure of decorin was analyzed to identify peptides that are representative of the inner and outer surface, and it was shown that only peptides based on the inner surface of decorin bind to collagen. The peptide with the highest binding affinity for collagenI, LHERHLNNN, served to slow down the diffusion of a conjugated dye in a collagen gel, while its dimer could physically crosslink collagen, thereby enhancing the elastic modulus of the gel by one order of magnitude. These results show the potential of the identified peptides for the design of biomaterials for applications in regenerative medicine.},
  language  = {en}
}
@article{SeckerBrosnanLuxenhoferetal.2015,
  author    = {Secker, Christian and Brosnan, Sarah M. and Luxenhofer, Robert and Schlaad, Helmut},
  title     = {Poly(alpha-Peptoid)s Revisited: Synthesis, Properties, and Use as Biomaterial},
  series = {Macromolecular bioscience},
  volume    = {15},
  journal   = {Macromolecular bioscience},
  number    = {7},
  publisher = {Wiley-VCH},
  address   = {Weinheim},
  issn      = {1616-5187},
  doi       = {10.1002/mabi.201500023},
  pages     = {881 -- 891},
  year      = {2015},
  abstract  = {Polypeptoids have been of great interest in the polymer science community since the early half of the last century; however, they had been basically forgotten materials until the last decades in which they have enjoyed an exciting revival. In this mini-review, we focus on the recent developments in polypeptoid chemistry, with particular focus on polymers synthesized by the ring-opening polymerization (ROP) of amino acid N-carboxyanhydrides (NCAs). Specifically, we will review traditional monomer synthesis (such as Leuchs, Katchalski, and Kricheldorf) and recent advances in polymerization methods to yield both linear, cyclic, and functional polymers, solution and bulk thermal properties, and preliminary results on the use of polypeptoids as biomaterials (i.e immunogenicity, biodistribution, degradability, and drug delivery).},
  language  = {en}
}
@article{HaralampievMertensSchwarzeretal.2015,
  author    = {Haralampiev, Ivan and Mertens, Monique and Schwarzer, Roland and Herrmann, Andreas and Volkmer, Rudolf and Wessig, Pablo and Mueller, Peter},
  title     = {Recruitment of SH-Containing peptides to lipid and biological membranes through the use of a palmitic acid functionalized with a Maleimide Group},
  series = {Angewandte Chemie : a journal of the Gesellschaft Deutscher Chemiker ; International edition},
  volume    = {54},
  journal   = {Angewandte Chemie : a journal of the Gesellschaft Deutscher Chemiker ; International edition},
  number    = {1},
  publisher = {Wiley-VCH},
  address   = {Weinheim},
  issn      = {1433-7851},
  doi       = {10.1002/anie.201408089},
  pages     = {323 -- 326},
  year      = {2015},
  abstract  = {This study presents a novel and easily applicable approach to recruit sulfhydryl-containing biomolecules to membranes by using a palmitic acid which is functionalized with a maleimide group. Notably, this strategy can also be employed with preformed (biological) membranes. The applicability of the assay is demonstrated by characterizing the binding of a Rhodamine-labeled peptide to lipid and cellular membranes using methods of fluorescence spectroscopy, lifetime measurement, and microscopy. Our approach offers new possibilities for preparing biologically active liposomes and manipulating living cells.},
  language  = {en}
}