@article{VacogneSchlaad2017,
  author    = {Vacogne, Charlotte D. and Schlaad, Helmut},
  title     = {Controlled ring-opening polymerization of alpha-amino acid N-carboxyanhydrides in the presence of tertiary amines},
  series = {Polymer : the international journal for the science and technology of polymers},
  volume    = {124},
  journal   = {Polymer : the international journal for the science and technology of polymers},
  publisher = {Elsevier},
  address   = {Oxford},
  issn      = {0032-3861},
  doi       = {10.1016/j.polymer.2017.07.062},
  pages     = {203 -- 209},
  year      = {2017},
  abstract  = {The mechanism of the primary ammonium/tertiary amine-mediated ring-opening polymerization of gamma-benzyl-L-glutamate N-carboxyanhydride (BLG-NCA) was investigated. Kinetic analyses revealed that the normal amine mechanism (NAM) together with a dormant-active chain end equilibrium were responsible for the controlled nature of this polymerization pathway, but that the polymerization also proceeded via the activated monomer mechanism (AMM). Mixtures of primary amines (1 equiv) and tertiary amines (0-1.5 equiv) were therefore tested to confirm the co-existence of the NAM and AMM and determine the limits for a controlled polymerization. For tertiary amine molar fractions smaller than 0.8 equiv, the reaction times were greatly reduced (compared to primary amine-initiated polymerization) without compromising the control of the reaction. Hence, the polymerization of NCA can proceed in a controlled manner even when the AMM contributes to the overall chain growth mechanism. (C) 2017 Elsevier Ltd. All rights reserved.},
  language  = {en}
}
@phdthesis{Vacogne2016,
  author    = {Vacogne, Charlotte D.},
  title     = {New synthetic routes towards well-defined polypeptides, morphologies and hydrogels},
  url       = {http://nbn-resolving.de/urn:nbn:de:kobv:517-opus4-396366},
  school      = {Universit{\"a}t Potsdam},
  pages     = {xii, 175},
  year      = {2016},
  abstract  = {Proteins are natural polypeptides produced by cells; they can be found in both animals and plants, and possess a variety of functions. One of these functions is to provide structural support to the surrounding cells and tissues. For example, collagen (which is found in skin, cartilage, tendons and bones) and keratin (which is found in hair and nails) are structural proteins. When a tissue is damaged, however, the supporting matrix formed by structural proteins cannot always spontaneously regenerate. Tailor-made synthetic polypeptides can be used to help heal and restore tissue formation. Synthetic polypeptides are typically synthesized by the so-called ring opening polymerization (ROP) of α-amino acid N-carboxyanhydrides (NCA). Such synthetic polypeptides are generally non-sequence-controlled and thus less complex than proteins. As such, synthetic polypeptides are rarely as efficient as proteins in their ability to self-assemble and form hierarchical or structural supramolecular assemblies in water, and thus, often require rational designing. In this doctoral work, two types of amino acids, γ-benzyl-L/D-glutamate (BLG / BDG) and allylglycine (AG), were selected to synthesize a series of (co)polypeptides of different compositions and molar masses. A new and versatile synthetic route to prepare polypeptides was developed, and its mechanism and kinetics were investigated. The polypeptide properties were thoroughly studied and new materials were developed from them. In particular, these polypeptides were able to aggregate (or self-assemble) in solution into microscopic fibres, very similar to those formed by collagen. By doing so, they formed robust physical networks and organogels which could be processed into high water-content, pH-responsive hydrogels. Particles with highly regular and chiral spiral morphologies were also obtained by emulsifying these polypeptides. Such polypeptides and the materials derived from them are, therefore, promising candidates for biomedical applications.},
  language  = {en}
}