Fluorescent IGF-II analogues for FRET-based investigations into the binding of IGF-II to the IGF-1R

Jade Cottam Jones, Paul Harris, Denis Scanlon, Briony Forbes, Margaret Brimble, Andrew Abell

    Research output: Contribution to journalArticlepeer-review

    5 Citations (Scopus)

    Abstract

    The interaction of IGF-II with the insulin receptor (IR) and type 1 insulin-like growth factor receptor (IGF-1R) has recently been identified as potential therapeutic target for the treatment of cancer. Understanding the interactions of IGF-II with these receptors is required for the development of potential anticancer therapeutics. This work describes an efficient convergent synthesis of native IGF-II and two non-native IGF-II analogues with coumarin fluorescent probes incorporated at residues 19 and 28. These fluorescent analogues bind with nanomolar affinities to the IGF-1R and are suitable for use in fluorescence resonance energy transfer (FRET) studies. From these studies the F19Cou IGF-II and F28Cou IGF-II proteins were identified as good probes for investigating the binding interactions of IGF-II with the IGF-1R and its other high affinity binding partners.

    Original languageEnglish
    Pages (from-to)2698-2705
    Number of pages8
    JournalOrganic and Biomolecular Chemistry
    Volume14
    Issue number9
    DOIs
    Publication statusPublished - 2016

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