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Issue 3, 2017

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

Supplementary files

Article information


Submitted
14 Sep 2016
Accepted
29 Oct 2016
First published
01 Nov 2016

This article is Open Access
All publication charges for this article have been paid for by the Royal Society of Chemistry

Chem. Sci., 2017,8, 1922-1926
Article type
Edge Article

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

This article is licensed under a Creative Commons Attribution 3.0 Unported Licence. You can use material from this article in other publications without requesting further permissions from the RSC, provided that the correct acknowledgement is given.

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