Biotinyl analogues of amylin as biologically active probes for amylin/CGRP receptor recognition

Andrew Chantry, Elizabeth A. Foot, Brendan Leighton, Anthony J. Day, Antony C. Willis

    Research output: Contribution to journalArticlepeer-review

    Abstract

    Biotinyl analogues of rat amylin were synthesised with sulfosuccinimidyl 2-(biotinamido)ethyl-1,3-dithiopropionate(NHS-SS-Biotin). Biotinylated amylin peptides were purified by HPLC, quantitated, and the presence of the biotin group at Lys-1 confirmed by peroxidase-labelled avidin and FAB mass spectroscopy. Amylin-biotin retained a similar affinity for binding to rat liver plasma membranes compared with rat amylin and also completely inhibited insulin-stimulated glycogen synthesis in rat soleus muscle incubated in vitro. These biologically active amylin probes will enable a complete analysis of amylin/CGRP receptor expression in various cell types and facilitate the isolation and characterisation of the hormone-receptor complex. © 1992.
    Original languageEnglish
    Pages (from-to)123-127
    Number of pages4
    JournalFEBS Letters
    Volume296
    Issue number2
    DOIs
    Publication statusPublished - 20 Jan 1992

    Keywords

    • Amylin
    • Biotinylation
    • CGRP
    • Non-insulin-dependent diabetes mellitus
    • Receptor

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