Chemical synthesis of a fluorescent IGF-II analogue

Jade Cottam, Denis Scanlon, John Karas, Antonio Calabrese, Tara Pukala, Briony Forbes, John Wallace, Andrew Abell

    Research output: Contribution to journalArticlepeer-review

    4 Citations (Scopus)

    Abstract

    Insulin-like growth factor II (IGF-II) is a protein with high structural and sequence similarity to insulin. Unlike insulin, it binds both the type 1 IGF receptor and the exon 11- isoform of the insulin receptor with high affinity. The overexpression and up regulation of IGF-II has been associated with the progression of various forms of cancer. The exact binding mechanism of IGF-II to its high affinity receptors is still not completely understood. Herein we describe the successful synthesis of a novel fluorescent IGF-II protein (F19Cou IGF-II), where residue 19 (phenylalanine) has been replaced by a fluorescent chromophore (coumaryl glycine). This novel coumaryl IGF-II analogue will be a useful tool for analysing the receptor interaction mechanisms in future studies.

    Original languageEnglish
    Pages (from-to)61-69
    Number of pages9
    JournalInternational Journal of Peptide Research and Therapeutics
    Volume19
    Issue number1
    DOIs
    Publication statusPublished - Mar 2013

    Keywords

    • Aggregation
    • Coumarin
    • Insulin-like growth factor II
    • Pseudoproline
    • Solid phase peptide synthesis

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