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  • Synthesis of Functional Characterization of Protein Domains for the Development of Mirror-Image Therapeutics

    Synthesis of Functional Characterization of Protein Domains for the Development of Mirror-Image Therapeutics by Iwamoto, Naoya;

    Series: Springer Theses;

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      • Publisher's listprice EUR 192.59
      • The price is estimated because at the time of ordering we do not know what conversion rates will apply to HUF / product currency when the book arrives. In case HUF is weaker, the price increases slightly, in case HUF is stronger, the price goes lower slightly.

        79 876 Ft (76 073 Ft + 5% VAT)
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      • Discounted price 63 901 Ft (60 858 Ft + 5% VAT)

    79 876 Ft

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    Product details:

    • Publisher Springer Nature Singapore
    • Date of Publication 5 February 2026

    • ISBN 9789819553655
    • Binding Hardback
    • No. of pages67 pages
    • Size 235x155 mm
    • Language English
    • Illustrations X, 67 p. 41 illus., 35 illus. in color.
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    Long description:

    This book focuses on the chemical synthesis and functional evaluations of several protein domains of therapeutic importance. The mirror-image protein domains, which can be prepared by chemical synthesis, are useful for the development of mirror-image protein therapeutics with low immunogenicity.

    This book first describes the preparation of two protein domains of therapeutic targets, the extracellular domain of T cell immunoreceptor with immunoglobulin and immunoreceptor tyrosine-based inhibitory motif domain (TIGIT), and human serum albumin domain III. The bioactivities and functions of these synthetic protein domains were confirmed by analyzing the interaction with their protein ligands and molecular probes. The mirror-image forms of these protein domains are applicable to screening campaigns by mirror-image phage display technology. Second, the design and synthesis of a novel variant of monobody, an antibody-like protein domain, are described. The monobody variant was prepared by facile synthetic procedures, enabling the practical synthesis of less-immunogenic mirror-image monobody. The variant was additionally applied to a structure–activity relationship study to explore the appropriate chemical modification for a superior monobody scaffold with improved stability and binding affinity.

    These data of the synthesis and evaluation of the protein domains in this book provide an important resource for studies on functional mirror-image protein domains for next-generation protein therapeutics.

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    Table of Contents:

    Chapter 1. Introduction.- Chapter 2 Synthetic Studies on the Extracellular Domain of the T Cell Immunoreceptor with Immunoglobulin and Immunoreceptor Tyrosine-Based Inhibitory Motif Domain (TIGIT) using Trt-K10 Solubilizing Tags.- Chapter 3 Mirror-Image Human Serum Albumin Domain III as a Tool for Analyzing Site II- Dependent Molecular Recognition.- Chapter 4 Development of Monobody Variants for Functional Mirror-Image Protein Therapeutics.- Chapter 5 Conclusion.

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