Please use this identifier to cite or link to this item: http://hdl.handle.net/2440/99395
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Type: Journal article
Title: Fluorescent IGF-II analogues for FRET-based investigations into the binding of IGF-II to the IGF-1R
Author: Cottam Jones, J.
Harris, P.
Scanlon, D.
Forbes, B.
Brimble, M.
Abell, A.
Citation: Organic and Biomolecular Chemistry, 2016; 14(9):2698-2705
Publisher: Royal Society of Chemistry
Issue Date: 2016
ISSN: 1477-0520
1477-0539
Statement of
Responsibility: 
J. M. Cottam Jones, P. W. R. Harris, D. B. Scanlon, B. E. Forbes, M. A. Brimble and A. D. Abell
Abstract: The interaction of IGF-II with the insulin receptor (IR) and type 1 insulin-like growth factor receptor (IGF-1R) has recently been identified as potential therapeutic target for the treatment of cancer. Understanding the interactions of IGF-II with these receptors is required for the development of potential anticancer therapeutics. This work describes an efficient convergent synthesis of native IGF-II and two non-native IGF-II analogues with coumarin fluorescent probes incorporated at residues 19 and 28. These fluorescent analogues bind with nanomolar affinities to the IGF-1R and are suitable for use in fluorescence resonance energy transfer (FRET) studies. From these studies the F19Cou IGF-II and F28Cou IGF-II proteins were identified as good probes for investigating the binding interactions of IGF-II with the IGF-1R and its other high affinity binding partners.
Keywords: Receptor, IGF Type 1; Insulin-Like Growth Factor II; Fluorescence Resonance Energy Transfer; Binding Sites; Molecular Structure; Fluorescence
Rights: Copyright status unknown
RMID: 0030042822
DOI: 10.1039/c5ob02110c
Appears in Collections:Chemistry publications

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