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

doi:10.1016/0014-5793(92)80362-K

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 journal › Article › peer-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 language	English
Pages (from-to)	123-127
Number of pages	4
Journal	FEBS Letters
Volume	296
Issue number	2
DOIs	https://doi.org/10.1016/0014-5793(92)80362-K
Publication status	Published - 20 Jan 1992

Keywords

Amylin
Biotinylation
CGRP
Non-insulin-dependent diabetes mellitus
Receptor

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1016/0014-5793(92)80362-K

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title = "Biotinyl analogues of amylin as biologically active probes for amylin/CGRP receptor recognition",

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. {\textcopyright} 1992.",

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author = "Andrew Chantry and Foot, {Elizabeth A.} and Brendan Leighton and Day, {Anthony J.} and Willis, {Antony C.}",

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doi = "10.1016/0014-5793(92)80362-K",

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TY - JOUR

T1 - Biotinyl analogues of amylin as biologically active probes for amylin/CGRP receptor recognition

AU - Chantry, Andrew

AU - Foot, Elizabeth A.

AU - Leighton, Brendan

AU - Day, Anthony J.

AU - Willis, Antony C.

PY - 1992/1/20

Y1 - 1992/1/20

N2 - 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.

AB - 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.

KW - Amylin

KW - Biotinylation

KW - CGRP

KW - Non-insulin-dependent diabetes mellitus

KW - Receptor

U2 - 10.1016/0014-5793(92)80362-K

DO - 10.1016/0014-5793(92)80362-K

M3 - Article

C2 - 1310286

VL - 296

SP - 123

EP - 127

JO - FEBS Letters

JF - FEBS Letters

SN - 0014-5793

IS - 2

ER -

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

Abstract

Keywords

UN SDGs

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