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Issue 12, 2016
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Converting disulfide bridges in native peptides to stable methylene thioacetals

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Abstract

Disulfide bridges play a crucial role in defining and rigidifying the three-dimensional structure of peptides. However, disulfides are inherently unstable in reducing environments. Consequently, the development of strategies aiming to circumvent these deficiencies – ideally with little structural disturbance – are highly sought after. Herein, we report a simple protocol converting the disulfide bond of peptides into highly stable methylene thioacetal. The transformation occurs under mild, biocompatible conditions, enabling the conversion of unprotected native peptides into analogues with enhanced stability. The developed protocol is applicable to a range of peptides and selective in the presence of a multitude of potentially reactive functional groups. The thioacetal modification annihilates the reductive lability and increases the serum, pH and temperature stability of the important peptide hormone oxytocin. Moreover, it is shown that the biological activities for oxytocin are retained.

Graphical abstract: Converting disulfide bridges in native peptides to stable methylene thioacetals

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Publication details

The article was received on 23 May 2016, accepted on 24 Jul 2016 and first published on 28 Jul 2016


Article type: Edge Article
DOI: 10.1039/C6SC02285E
Citation: Chem. Sci., 2016,7, 7007-7012
  • Open access: Creative Commons BY-NC license
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    Converting disulfide bridges in native peptides to stable methylene thioacetals

    C. M. B. K. Kourra and N. Cramer, Chem. Sci., 2016, 7, 7007
    DOI: 10.1039/C6SC02285E

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