Noncovalent Tagging Proteins with Paramagnetic Lanthanide Complexes for Protein Study

Authors

  • Zhen Wei,

    1. State Key Laboratory of Elemento-Organic Chemistry and College of Chemistry, Nankai University, Weijin Road 94, Tianjin 300071 (P.R. China), Fax: (+86) 22-23500623
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    • These authors contributed equally to this work.

  • Yin Yang,

    1. State Key Laboratory of Elemento-Organic Chemistry and College of Chemistry, Nankai University, Weijin Road 94, Tianjin 300071 (P.R. China), Fax: (+86) 22-23500623
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    • These authors contributed equally to this work.

  • Qing-Feng Li,

    1. State Key Laboratory of Elemento-Organic Chemistry and College of Chemistry, Nankai University, Weijin Road 94, Tianjin 300071 (P.R. China), Fax: (+86) 22-23500623
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  • Feng Huang,

    1. State Key Laboratory of Elemento-Organic Chemistry and College of Chemistry, Nankai University, Weijin Road 94, Tianjin 300071 (P.R. China), Fax: (+86) 22-23500623
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  • Hui-Hui Zuo,

    1. State Key Laboratory of Elemento-Organic Chemistry and College of Chemistry, Nankai University, Weijin Road 94, Tianjin 300071 (P.R. China), Fax: (+86) 22-23500623
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  • Prof. Xun-Cheng Su

    Corresponding author
    1. State Key Laboratory of Elemento-Organic Chemistry and College of Chemistry, Nankai University, Weijin Road 94, Tianjin 300071 (P.R. China), Fax: (+86) 22-23500623
    • State Key Laboratory of Elemento-Organic Chemistry and College of Chemistry, Nankai University, Weijin Road 94, Tianjin 300071 (P.R. China), Fax: (+86) 22-23500623
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Abstract

The site-specific labeling of proteins with paramagnetic lanthanides offers unique opportunities for NMR spectroscopic analysis in structural biology. Herein, we report an interesting way of obtaining paramagnetic structural restraints by employing noncovalent interaction between a lanthanide metal complex, [Ln(L)3]n (L=derivative of dipicolinic acid, DPA), and a protein. These complexes formed by lanthanides and DPA derivatives, which have different substitution patterns on the DPA derivatives, produce diverse thermodynamic and paramagnetic properties when interacting with proteins. The binding affinity of [Ln(L)3]n with proteins, as well as the determined paramagnetic tensor, are tunable by changing the substituents on the ligands. These noncovalent interactions between [Ln(L)3]n and proteins offer great opportunities in the tagging of proteins with paramagnetic lanthanides. We expect that this method will be useful for obtaining multiple angles and distance restraints of proteins in structural biology.

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