Reagentless Oxidative Folding of Disulfide-Rich Peptides Catalyzed by an Intramolecular Diselenide

Authors

  • Andrew M. Steiner,

    1. Department of Medicinal Chemistry, University of Utah, 421 Wakara Way, Suite 360, Salt Lake City, UT 84108 (USA)
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  • Prof. Dr. Kenneth J. Woycechowsky,

    1. Department of Chemistry, University of Utah, 315 S. 1400 E., Rm. 1320, Salt Lake City, UT 84112 (USA)
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  • Prof. Dr. Baldomero M. Olivera,

    1. Department of Biology, University of Utah, 257 S. 1400 E., Rm. 115, Salt Lake City, UT 84112 (USA)
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  • Prof. Dr. Grzegorz Bulaj

    Corresponding author
    1. Department of Medicinal Chemistry, University of Utah, 421 Wakara Way, Suite 360, Salt Lake City, UT 84108 (USA)
    • Department of Medicinal Chemistry, University of Utah, 421 Wakara Way, Suite 360, Salt Lake City, UT 84108 (USA)
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  • We thank Professors David Blair, David Goldenberg, and Donald Hilvert for helpful discussions and comments on the manuscript. We also acknowledge the assistance of the Peptide Synthesis and Mass Spectrometry Core Facilities at the University of Utah. This work was supported by the NIH Program Project Grant GM 48677.

Abstract

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Brückenbau: In cysteinreichen Peptiden können Diselenide als Ersatz für Disulfidbrücken dienen, da die energetische Bevorzugung von Se-Se- gegenüber gemischten Se-S-Brücken die Faltung vereinfacht (siehe Bild). Eine intramolekulare Diselenidbrücke katalysiert die oxidative Faltung von Selenopeptidanaloga von Conotoxinen und bietet eine reagenslose Methode, um die Bildung verschiedener nativer Disulfidbrückenmuster zu beschleunigen.

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