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  • 1
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    Nature Publishing Group (NPG)
    Publication Date: 2008-03-07
    Description: Polysaccharide-based hydrogels are useful for numerous applications, from food and cosmetic processing to drug delivery and tissue engineering. The formation of hydrogels from polyelectrolyte solutions is complex, involving a variety of molecular interactions. The physical gelation of polysaccharides can be achieved by balancing solvophobic and solvophilic interactions. Polymer chain reorganization can be obtained by solvent exchange, one of the processing routes forming a simple hydrogel assembly. Nevertheless, many studies on hydrogel formation are empirical with a limited understanding of the mechanisms involved, delaying the processing of more complex structures. Here we use a multi-step interrupted gelation process in controlled physico-chemical conditions to generate complex hydrogels with multi-membrane 'onion-like' architectures. Our approach greatly simplifies the processing of gels with complex shapes and a multi-membrane organization. In contrast with existing assemblies described in the literature, our method allows the formation of free 'inter-membrane' spaces well suited for cell or drug introduction. These architectures, potentially useful in biomedical applications, open interesting perspectives by taking advantage of tailor-made three-dimensional multi-membrane tubular or spherical structures.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ladet, Sebastien -- David, Laurent -- Domard, Alain -- England -- Nature. 2008 Mar 6;452(7183):76-9. doi: 10.1038/nature06619.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Universite de Lyon, Universite Lyon 1, UMR CNRS 5223, Ingenierie des Materiaux Polymeres (IMP), Laboratoire des Materiaux Polymeres et des Biomateriaux, 15 Boulevard A. Latarjet, Batiment ISTIL, F-69622 Villeurbanne Cedex, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18322531" target="_blank"〉PubMed〈/a〉
    Keywords: Alcohols/chemistry ; Alginates/chemistry ; Animals ; Chitosan/*chemistry ; Decapodiformes ; Electrolytes/chemistry ; Hydrogels/*chemistry ; Hydrophobic and Hydrophilic Interactions ; Solvents/chemistry ; Viscosity
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
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  • 2
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    International Journal of Biological Macromolecules 12 (1990), S. 289-294 
    ISSN: 0141-8130
    Keywords: Chitosan ; electron diffraction ; shish-kebab morphology ; single crystals
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    International Journal of Biological Macromolecules 9 (1987), S. 333-336 
    ISSN: 0141-8130
    Keywords: Chitosan ; N-acetylation ; circular dichroism
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 1432-2048
    Keywords: Chitosan ; Glucosamine oligomer binding ; Lectin ; Rubus (cell suspension)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A lectin specific for glucosamine oligomers has been purified by chitosan affinity chromatography from cultured cells of Rubus. The lectin, eluted by a glucosamine oligomer of degree of polymerization 4 in the presence of l-α-phosphatidylserine dipalmitoyl, was found by sodium dodecyl sulfate-polyacrylamide gel electroploresis to be homogeneous and to have a molecular weight of 67 kilodaltons; it could best bind the tetrasaccharide, as shown by ligand-blot processing. Data from kinetic-dependent enzyme-linked immunosorbent assays showed that the lectin has two apparent binding sites which better accommodate the tetrasaccharide and the hexasaccharide, respectively, of the glucosamineoligomer series. The affinity of the lectin for glucosamine oligomers was shown to decrease for chain lengths greater than six glucosaminyl residues.
    Type of Medium: Electronic Resource
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