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Now showing 1 - 5 of 5
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    Supramolecular assemblies of block copolymers as templates for fabrication of nanomaterials
    (New York, NY [u.a.] : Elsevier, 2011) Nandan, B.; Kuila, B.K.; Stamm, M.
    Self-assembled polymeric systems have played an important role as templates for nanofabrication; they offer nanotemplates with different morphologies and tunable sizes, are easily removed after reactions, and could be further modified with different functional groups to enhance the interactions. Among the various self-assembled polymeric systems, block copolymer supramolecular assemblies have received considerable attention because of the inherent processing advantages. These supramolecular assemblies are formed by the non-covalent interactions of one of the blocks of the block copolymer with a low molar-mass additive. Selective extraction of the additive leads to porous membranes or nano-objects which could then be used as templates for nanofabrication leading to a variety of ordered organic/inorganic nanostructures. In this feature article, we present an over-view of the recent developments in this area with a special focus on some examples from our group.
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    Amyloids: From molecular structure to mechanical properties
    (Amsterdam [u.a.] : Elsevier, 2013) Schleeger, M.; Vandenakker, C.C.; Deckert-Gaudig, T.; Deckert, V.; Velikov, K.P.; Koenderink, G.; Bonn, M.
    Many proteins of diverse sequence, structure and function self-assemble into morphologically similar fibrillar aggregates known as amyloids. Amyloids are remarkable polymers in several respects. First of all, amyloids can be formed from proteins with very different amino acid sequences; the common denominator is that the individual proteins constituting the amyloid fold predominantly into a β-sheet structure. Secondly, the formation of the fibril occurs through non-covalent interactions between primarily the β-sheets, causing the monomers to stack into fibrils. The fibrils are remarkably robust, considering that the monomers are bound non-covalently. Finally, a common characteristic of fibrils is their unbranched, straight, fiber-like structure arising from the intertwining of the multiple β-sheet filaments. These remarkably ordered and stable nanofibrils can be useful as building blocks for protein-based functional materials, but they are also implicated in severe neurodegenerative diseases. The overall aim of this article is to highlight recent efforts aimed at obtaining insights into amyloid proteins on different length scales. Starting from molecular information on amyloids, single fibril properties and mechanical properties of networks of fibrils are described. Specifically, we focus on the self-assembly of amyloid protein fibrils composed of peptides and denatured model proteins, as well as the influence of inhibitors of fibril formation. Additionally, we will demonstrate how the application of recently developed vibrational spectroscopic techniques has emerged as a powerful approach to gain spatially resolved information on the structure-function relation of amyloids. While spectroscopy provides information on local molecular conformations and protein secondary structure, information on the single fibril level has been developed by diverse microscopic techniques. The approaches to reveal basic mechanical properties of single fibrils like bending rigidity, shear modulus, ultimate tensile strength and fracture behavior are illustrated. Lastly, mechanics of networks of amyloid fibrils, typically forming viscoelastic gels are outlined, with a focus on (micro-) rheological properties. The resulting fundamental insights are essential for the rational design of novel edible and biodegradable protein-based polymers, but also to devise therapeutic strategies to combat amyloid assembly and accumulation during pathogenic disorders.
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    Hydrogel-based actuators: Possibilities and limitations
    (Amsterdam [u.a.] : Elsevier, 2014) Ionov, L.
    The rapid development of microtechnology in recent times has increased the necessity for the development of devices, which are able to perform mechanical work on the micro- and macroscale. Among all kinds of actuators, the ones based on stimuli-responsive hydrogels, which are three-dimensional polymer networks strongly imbibed with water, deserve particular attention. This paper aims to provide a brief overview of stimuli-responsive hydrogel actuators with respect to their sensitivity to different stimuli, different kinds of deformation, the possibilities of generating different types of movement, as well as their applications.
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    Microfluidic fabrication of polyethylene glycol microgel capsules with tailored properties for the delivery of biomolecules
    (Cambridge : RSC, 2017) Guerzoni, Luis P. B.; Bohl, Jan; Jans, Alexander; Rose, Jonas C.; Koehler, Jens; Kuehne, Alexander J. C.; De Laporte, Laura
    Microfluidic encapsulation platforms have great potential not only in pharmaceutical applications but also in the consumer products industry. Droplet-based microfluidics is increasingly used for the production of monodisperse polymer microcapsules for biomedical applications. In this work, a microfluidic technique is developed for the fabrication of monodisperse double emulsion droplets, where the shell is crosslinked into microgel capsules. A six-armed acrylated star-shaped poly(ethylene oxide-stat-propylene oxide) pre-polymer is used to form the microgel shell after a photo-initiated crosslinking reaction. The synthesized microgel capsules are hollow, enabling direct encapsulation of large amounts of multiple biomolecules with the inner aqueous phase completely engulfed inside the double emulsion droplets. The shell thickness and overall microgel sizes can be controlled via the flow rates. The morphology and size of the shells are characterized by cryo-SEM. The encapsulation and retention of 10 kDa FITC-dextran and its microgel degradation mediated release are monitored by fluorescence microscopy. © 2017 The Royal Society of Chemistry.
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    Reconstitution properties of biologically active polymersomes after cryogenic freezing and a freeze-drying process
    (London : RSC Publishing, 2018) Ccorahua, Robert; Moreno, Silvia; Gumz, Hannes; Sahre, Karin; Voit, Brigitte; Appelhans, Dietmar
    Reconstitution of biologically active polymersomes from the frozen or solid state into any fluid state is still a challenging issue for the design of new biological experiments and for the formulation of therapeutic agents. To gain knowledge about the reconstitution of pH-responsive and photo-crosslinked polymersomes, surface-functionalized and enzyme-containing polymersomers were cryogenically frozen (-20 °C) or freeze-dried with inulin as the lyoprotectant (0.1% w/v) and stored for a defined time period. Reconstituting those polymersomes in solution by thawing or a re-dispersing process revealed their original physical properties as well as their function as a pH-switchable enzymatic nanoreactor.