Supplementary Material for Chemical Communications
This journal is © The Royal Society of Chemistry 2003
Supplementary Information
A/A 0 at 260 nm
1.3
1.2
1.1
1
0
10
20
30
40
Time / min
50
60
Fig. S1 A time course of absorbance increase of the ligated nucleo-nanocages 1-3, due to the
enzymatic action of DNase I. [nucleobase] = 30 µM, enzyme, 30 unit in 330 µL of 20 mM Tris-HCl
buffer (pH 7.5, containing 0.5 M NaCl, 1 mM CaCl2, and 1 mM MgCl2) at 37 °C. Absorption
changes were monitored at 260 nm.
As shown in Figure S1, the ligated nucleo-nanocages are readily digested with DNase I
under the standard condition. Molecular weight of DNase I is 29 kDa, which is
comparable to these of exonuclease III (31 kDa) and mung bean nuclease (39 kDa).
Therefore, it is reasonable to assume that the observed resistance towards exonuclease
III and mung bean nuclease are ascribed to the absence of end structures, but not to the
steric hindrance.