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Issue 3, 2017
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Accessing human selenoproteins through chemical protein synthesis

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Abstract

The human body contains 25 selenoproteins, which contain in their sequence the twenty-first encoded amino acid, selenocysteine. About a dozen of these proteins remain functionally uncharacterized or poorly studied. Challenges in accessing these selenoproteins using traditional recombinant expressions have prevented biological characterization thus far. Chemical protein synthesis has the potential to overcome these hurdles. Here we report the first total chemical syntheses of two human selenoproteins, selenoprotein M (SELM) and selenoprotein W (SELW). The synthesis of the more challenging protein SELM was enabled using recent advances in the field of selenocysteine chemistry. This approach allows the preparation of selenoproteins in milligram quantities and in homogenous form, which should open new horizons for future studies to pursue a fuller biological understanding of their role in health and disease.

Graphical abstract: Accessing human selenoproteins through chemical protein synthesis

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Publication details

The article was received on 14 Sep 2016, accepted on 29 Oct 2016 and first published on 01 Nov 2016


Article type: Edge Article
DOI: 10.1039/C6SC04123J
Citation: Chem. Sci., 2017,8, 1922-1926
  • Open access: Creative Commons BY license
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    Accessing human selenoproteins through chemical protein synthesis

    L. Dery, P. S. Reddy, S. Dery, R. Mousa, O. Ktorza, A. Talhami and N. Metanis, Chem. Sci., 2017, 8, 1922
    DOI: 10.1039/C6SC04123J

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