Second generation specific-enzyme-activated rotaxane propeptides

Fernandes, Antony;Viterisi, Aurélien;Aucagne, Vincent;Leigh, David A.;Papot, Sébastien
(2012) Chemical Communications — Vol. 48, n° 15, p. 2083-2085 (2012)

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Authors
  • Fernandes, AntonyUCLouvain
    Author
  • Viterisi, AurélienUniversity of Edinburgh
    Author
  • Aucagne, VincentCentre de biophysique moléculaire, Orléans, France
    Author
  • Leigh, David A.University of Edinburgh
    Author
  • Papot, SébastienUniversité de Poitiers
    Author
Abstract
A [2]rotaxane, in which the peptidic axle is protected from degradation by the macrocyclic sheath and terminated with a novel glycosidase-cleavable stopper, is rendered water-soluble by derivatisation with tetra(ethylene glycol) (TetEG) or glucosylated tetra(ethylene glycol) (Glc-TetEG) chains using the CuAAC ‘click’ reaction. The Glc-TetEG-derivatised rotaxane propeptide is >50 000 times more soluble in aqueous media than the parent rotaxane. Activation of the water-soluble rotaxane propeptide with a β-galactosidase efficiently releases the parent peptide.
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Fernandes, A., Viterisi, A., Aucagne, V., Leigh, D. A., & Papot, S. (2012). Second generation specific-enzyme-activated rotaxane propeptides. Chemical Communications, 48(15), 2083-2085. https://doi.org/10.1039/c2cc17458h (Original work published 2012)