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Issue 19, 2009
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ITAM-derived phosphopeptide-containing dendrimers as multivalent ligands for Syk tandem SH2 domain

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Abstract

Spleen tyrosine kinase (Syk) is activated when its tandem SH2 domain (tSH2) binds to a diphosphorylated ITAM motif of e.g. the FcεRI receptor. In this divalent interaction each SH2 domain binds to a phosphotyrosine-containing tetrapeptide motif in ITAM. One of those tetrapeptide sequences was synthesized and conjugated to dendrimersvia‘click’ chemistry to create a series of functional phosphopeptide-containing dendrimers ranging from a monovalent to an octavalent dendrimer. The affinity of the functionalized dendrimers for Syk tSH2 has been assayed in SPR competition experiments. Both the tetra- and octavalent dendrimer had an affinity in the high nanomolar range, which is approximately 100-fold enhanced compared to the monovalent tetrapeptide, indicating a multivalency effect.

Graphical abstract: ITAM-derived phosphopeptide-containing dendrimers as multivalent ligands for Syk tandem SH2 domain

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Publication details

The article was received on 25 Mar 2009, accepted on 02 Jul 2009 and first published on 07 Aug 2009


Article type: Paper
DOI: 10.1039/B905938E
Citation: Org. Biomol. Chem., 2009,7, 4088-4094

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    ITAM-derived phosphopeptide-containing dendrimers as multivalent ligands for Syk tandem SH2 domain

    J. Kuil, H. M. Branderhorst, R. J. Pieters, N. J. de Mol and R. M. J. Liskamp, Org. Biomol. Chem., 2009, 7, 4088
    DOI: 10.1039/B905938E

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