Biotinyl analogues of rat amylin were synthesised with sulfosu~inimidyl 2-(biotinamido) ethyl-1,3-dithiopropionate (N HS-SS-Biotin). Biotinylated amylin peptides were purified by HIaLC, quantltated, and the presence of the biotin group at Lys-I confirmed by peroxidase-labelled avidin and FAB mass spectroscopy. Amylin.biotin retained a similar affinity for binding to rat liver plasma membranes ¢.ompared with rat atnylin and also completely inhibited insulin-stimulated glycogen synthesis in rat soleus muscle incubated in vitro. These biologically active amylln probes will enable a complete analysis of anaylin/CGRP receptor er, pression in various cell types and facilitate the isolation and characterisation of the hormonereceptor complex.