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Biotinyl analogues of amylin as biologically active probes for amylin/CGRP receptor recognition
Author(s) -
Chantry Andrew,
Foot Elizabeth A.,
Leighton Brendan,
Day Anthony J.,
Willis Antony C.
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)80362-k
Subject(s) - amylin , chemistry , calcitonin gene related peptide , biological activity , receptor , biochemistry , endocrinology , biology , neuropeptide , diabetes mellitus , in vitro , islet
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.