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Issue 16, 2006
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A cationic lanthanide complex binds selectively to phosphorylated tyrosine sites, aiding NMR analysis of the phosphorylated insulin receptor peptide fragment

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Abstract

The binding of two cationic europium complexes to a differentially phosphorylated insulin receptor peptide has been studied by emission spectroscopy and 31P NMR and 1H NMR TOCSY methods. Analysis of the europium emission and NMR spectral data was consistent with the presence of species in slow exchange on the NMR and emission timescales, in agreement with selective binding of the lanthanide ion to the phospho-tyrosine site, allowing such complexes to be considered as prototypical chemoselective paramagnetic derivatising agents.

Graphical abstract: A cationic lanthanide complex binds selectively to phosphorylated tyrosine sites, aiding NMR analysis of the phosphorylated insulin receptor peptide fragment

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Publication details

The article was received on 15 Jun 2006, accepted on 30 Jun 2006 and first published on 19 Jul 2006


Article type: Paper
DOI: 10.1039/B608528H
Citation: Org. Biomol. Chem., 2006,4, 3166-3171
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    A cationic lanthanide complex binds selectively to phosphorylated tyrosine sites, aiding NMR analysis of the phosphorylated insulin receptor peptide fragment

    P. Atkinson, B. S. Murray and D. Parker, Org. Biomol. Chem., 2006, 4, 3166
    DOI: 10.1039/B608528H

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