A cationic lanthanide complex binds selectively to phosphorylated tyrosine sites, aiding NMR analysis of the phosphorylated insulin receptor peptide fragment
A cationic lanthanide complex binds selectively to phosphorylated tyrosine sites, aiding NMR analysis of the phosphorylated insulin receptor peptide fragment
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DOI：
10.1039/b608528h
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发表时间：
2006-01-01
影响因子：
3.2
通讯作者：
Parker, David
中科院分区：
文献类型：
--
作者：
Atkinson, Paul;Murray, Benjamin S.;Parker, David
用发射光谱、P-31核磁共振和H-1核磁共振TOCSY方法研究了两种阳离子铕配合物与差异磷酸化的胰岛素受体肽的结合。对铕发射和核磁共振光谱数据的分析与在核磁共振和发射时间尺度上缓慢交换的物质的存在一致，与镧系离子与磷酸酪氨酸位点的选择性结合一致，允许这种配合物被认为是典型的化学选择性顺磁衍生剂。
The binding of two cationic europium complexes to a differentially phosphorylated insulin receptor peptide has been studied by emission spectroscopy and P-31\ NMR and H-1 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.