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Titlebook: Bio-synthetic Polymer Conjugates; Helmut Schlaad Book 2013 Springer-Verlag Berlin Heidelberg 2013 Bioconjugates.Biohybrid materials.Click

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https://doi.org/10.1007/978-3-030-04534-0ides show secondary structure effects and specific non-covalent interactions, which can cause a specific aggregation behavior and result in interesting supramolecular structures. Conjugation of polypeptides with simple synthetic polymers combines these phenomena with the advantages of synthetic poly
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https://doi.org/10.1007/978-3-030-04534-0ntages in bio-applications. Over the past few years, numerous chemical strategies have been developed to conjugate different synthetic polymers onto proteins, most of which can be summarized within the scope of click-chemistry. Here we highlight conjugation strategies based on available functional g
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STS-119, Expeditions 18, 19 and 20, STS-127ers that have a wide range of biological recognition properties has grown rapidly in the last decade due to their application in the areas of biotechnology and medicinal chemistry. Modern synthetic methodologies such as controlled radical polymerization, ionic polymerization, ring-opening polymeriza
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https://doi.org/10.1007/978-3-030-04534-0roups present on the synthetic polymer and existing groups of proteins from the natural pool. In particular, the chapter organizes the various possible reactions by classes of functional groups present on protein surfaces, deriving from selected amino acid residues.
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0065-3195 each written by the world renowned experts.Still valid and Polypeptide-Polymer Conjugates, by Henning Menzel Chemical Strategies for the Synthesis of Protein-Polymer Conjugates, by Björn Jung and Patrick Theato Glycopolymer Conjugates, by Ahmed M. Eissa and Neil R. Cameron DNA-Polymer Conjugates: F
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,Chemical Strategies for the Synthesis of Protein–Polymer Conjugates,roups present on the synthetic polymer and existing groups of proteins from the natural pool. In particular, the chapter organizes the various possible reactions by classes of functional groups present on protein surfaces, deriving from selected amino acid residues.
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