Biomedical Engineering Reference
In-Depth Information
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0
0
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0
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1400
A
B
Time (s)
Time (s)
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Time (s)
Figure 11.10
Binding and dissociation (hybridization) of 5
M target in solution (a) complementary to CYP2C9*2,
(b) with a single base mismatch to CYP2C9*2 immobilized on an ion-sensitive field-effect
transistor-based biosensor, and (c) 5
m
M target DNA in solution to a single-mismatch
DNA, CYP2C9*1 immobilized on an ion-sensitive field-effect transistor-based biosensor
(
Uno et al., 2007
).
m
and immobilized on a SPR biosensor surface (
Uno et al., 2007
). A single-fractal analysis is
once again adequate to describe the binding and the dissociation kinetics. The values of
(a) the binding rate coefficient,
k
, and the fractal dimension,
D
f
, for a single-fractal analysis,
and (b) the dissociation rate coefficient,
k
d
, and the fractal dimension,
D
fd
, for a single-fractal
analysis are given in
Table 11.6
(a) and (b). In this case, the affinity,
K
(
¼k
/
k
d
), value is 3.954.
Figure 11.11a
and
Table 11.6
(a) and (b) show the increase in the binding rate coefficient,
k
,
with an increase in the fractal dimension,
D
f
, for a single-fractal analysis. For the data shown
in
Figure 11.11a
and
Table 11.6
(a) and (b), the binding rate coefficient,
k
, is given by:
10
07
10
07
D
10
:
91
3
:
59
k
¼ð
4
:
6
1
:
7
Þ
ð
11
:
5a
Þ
f
The fit is reasonable. Only three data points are available. The availability of more data
points would lead to a more reliable fit. The binding rate coefficient,
k
, for a single-fractal
analysis is very sensitive to the fractal dimension,
D
f
, or the degree of heterogeneity that
