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Peptidomimetic SH2 Domain Antagonists for Targeting Signal Transduction

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Bioorganic Chemistry of Biological Signal Transduction

Part of the book series: Topics in Current Chemistry ((TOPCURRCHEM,volume 211))

Abstract

Within the last few years, therapeutic intervention into signal transduction cascades attracted the interest of pharmaceutical research. Apart from selective inhibition of phosphorylating and dephosphorylating enzymes, medicinal chemistry has focused on an SH2 domain-targeted drug design approach. This review will briefly summarize the role of adaptor proteins in signaling networks, followed by an introduction on the functional and structural details of SH2 domains in terms of protein architecture and mode of ligand binding. Major emphasis is laid on medicinal chemistry programs that aim to develop peptidomimetic SH2 domain inhibitors. Different strategies for phosphotyrosine-replacement will be presented, followed by a detailed discussion of the iterative optimization cycles revealing new peptidomimetic and non-peptide SH2 domain antagonists. Finally, an outlook is given on further applications of the modular chemistry concept and the privileged building blocks, that have been developed in SH2 domain inhibitor programs, onto a new class of adaptor proteins, notably the PTB domains.

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  1. Central Research ZF-WFM, BAYER AG, Building Q18, 51368, Leverkusen, Germany

    Gerhard Müller

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  1. Gerhard Müller
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  1. Max-Planck-Institut für Molekulare Physiologie, Universität Dortmund, Otto-Hahn-Straße 11, 44221, Dortmund, Germany

    Herbert Waldmann

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This contribution is dedicated to Prof. Dr. Horst Kessler on the occasion of his 60th birthday.

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© 2000 Springer-Verlag Berlin Heidelberg

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Müller, G. (2000). Peptidomimetic SH2 Domain Antagonists for Targeting Signal Transduction. In: Waldmann, H. (eds) Bioorganic Chemistry of Biological Signal Transduction. Topics in Current Chemistry, vol 211. Springer, Berlin, Heidelberg. https://doi.org/10.1007/3-540-45035-1_2

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  • DOI: https://doi.org/10.1007/3-540-45035-1_2

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