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

Paul Atkinson; Benjamin S. Murray; David Parker

doi:10.1039/b608528h

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

Paul Atkinson
, Benjamin S. Murray
, David Parker^*

^*Corresponding author for this work

Department of Chemistry

Research output: Contribution to journal › Journal article › peer-review

33 Citations (Scopus)

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.

Original language	English
Pages (from-to)	3166-3171
Number of pages	6
Journal	Organic and Biomolecular Chemistry
Volume	4
Issue number	16
DOIs	https://doi.org/10.1039/b608528h
Publication status	Published - 19 Jul 2006

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10.1039/b608528h

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@article{44c2c3b3d5894be2b4149ad4dff5aedf,

title = "A cationic lanthanide complex binds selectively to phosphorylated tyrosine sites, aiding NMR analysis of the phosphorylated insulin receptor peptide fragment",

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.",

author = "Paul Atkinson and Murray, \{Benjamin S.\} and David Parker",

note = "We thank EPSRC and ESF-COST D18/D38 for support, and Professor Silvio Aime and his colleagues for preliminary studies in Ivrea examining the applicability of the method on neurotensin. Publisher copyright: {\textcopyright} The Royal Society of Chemistry 2006",

year = "2006",

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doi = "10.1039/b608528h",

language = "English",

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A cationic lanthanide complex binds selectively to phosphorylated tyrosine sites, aiding NMR analysis of the phosphorylated insulin receptor peptide fragment. / Atkinson, Paul; Murray, Benjamin S.; Parker, David.
In: Organic and Biomolecular Chemistry, Vol. 4, No. 16, 19.07.2006, p. 3166-3171.

Research output: Contribution to journal › Journal article › peer-review

TY - JOUR

T1 - A cationic lanthanide complex binds selectively to phosphorylated tyrosine sites, aiding NMR analysis of the phosphorylated insulin receptor peptide fragment

AU - Atkinson, Paul

AU - Murray, Benjamin S.

AU - Parker, David

N1 - We thank EPSRC and ESF-COST D18/D38 for support, and Professor Silvio Aime and his colleagues for preliminary studies in Ivrea examining the applicability of the method on neurotensin. Publisher copyright: © The Royal Society of Chemistry 2006

PY - 2006/7/19

Y1 - 2006/7/19

N2 - 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.

AB - 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.

UR - https://www.scopus.com/pages/publications/33746922377

U2 - 10.1039/b608528h

DO - 10.1039/b608528h

M3 - Journal article

C2 - 16886086

AN - SCOPUS:33746922377

SN - 1477-0520

VL - 4

SP - 3166

EP - 3171

JO - Organic and Biomolecular Chemistry

JF - Organic and Biomolecular Chemistry

IS - 16

ER -

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

Abstract

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