4.7 Article

Second generation specific-enzyme-activated rotaxane propeptides

Journal

CHEMICAL COMMUNICATIONS
Volume 48, Issue 15, Pages 2083-2085

Publisher

ROYAL SOC CHEMISTRY
DOI: 10.1039/c2cc17458h

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Funding

  1. Science and Technology Department of the French Embassy in the United Kingdom
  2. Scottish Executive
  3. Royal Society of Edinburgh and the Engineering and Physical Sciences Research Council (EPSRC)

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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 beta-galactosidase efficiently releases the parent peptide.

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