This work was supported by the Science and Technology
Department of the French Embassy in the United Kingdom,
the Scottish Executive, the Royal Society of Edinburgh and the
Engineering and Physical Sciences Research Council (EPSRC).
Notes and references
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Scheme 3 CuAAC post-functionalisation of rotaxane 1.
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Scheme 4 Propeptide thread 21 and rotaxane 22.
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Fig. 2 (a) Superimposed HPLC traces (l = 220 nm, reverse phase
C-18 column) of individual components 3, 6, 8 and 10. (b) and (c)
HPLC traces of the enzymatic hydrolysis of rotaxane propeptide 3
with E. coli b-galactosidase in phosphate buffer (0.02 M, pH 7.0) at
37 1C using 1000 U/mmol of substrate after (b) 2 h and (c) 10 h
(Scheme 1).
the CuAAC reaction. Both the novel self-immolative stopper
and the bis-azido rotaxane ring employed in this system may
prove useful for accessing a wide range of propeptides deco-
rated for specific biological applications.
12 The modest yield (24%) of 19 was largely the result of a challenging
purification procedure that required preparative reverse phase HPLC
to obtain the bis-TetEG-functionalised rotaxane in good purity.
c
This journal is The Royal Society of Chemistry 2012
Chem. Commun., 2012, 48, 2083–2085 2085