Biomedical Engineering Reference
In-Depth Information
Table 11.6: (a) Binding and dissociation rate coefficients and (b) fractal dimensions for the
binding and the dissociation phases for PNA-DNA hybridization (a) 5
M target DNA in
solution complementary to CYP2C9*2 as a probe PNA immobilized on a nucleic acid-modified
ion-selective field-effect transistor-based biosensor, and (b) target DNA in solution
complementary to CYP2C9*2 and with involvement of a single mismatch in either the target
DNA or the probe PNA immobilized on the nucleic acid-modified ion-selective field-effect
transistor-based biosensor (
Uno et al., 2007
).
m
(a)
Analyte in Solution/Receptor on Surface
k
k
d
5
m
M target DNA complementary to receptor, CYP2C9*2/probe
PNA, CYP2C9*2
131.10 8.02
0.00432 0.00099
Target DNA with single base mismatch/probe PNA, CYP2C9*2
57.253 2.398
0.2496 0.0310
Target DNA complementary to receptor/Probe PNSA,
CYP2C9*2 with a single mismatch
15.429
1.369
3.9020
0.344
(b)
Analyte in Solution/Receptor on Surface
D
f
D
fd
5
M target DNA complementary to receptor, CYP2C9*2/probe
PNA, CYP2C9*2
2.6306
0.0730
0.00432
0.00099
m
Target DNA with single base mismatch/probe PNA, CYP2C9*2
2.5712
0.00304
0.2496
0.0310
Target DNA complementary to receptor/Probe PNSA,
CYP2C9*2 with a single mismatch
2.6306 0.0703
0.102 þ 0.179
exists on the biosensor surface as noted by the close to eleventh (equal to 10.91) order of
dependence exhibited.
Figure 11.11b
and
Table 11.6
(a) and (b) show the increase in the dissociation rate coefficient,
k
d
with an increase in the fractal dimension,
D
fd
, for a single-fractal analysis. For the data shown in
Figure 11.11a
and
Table 11.6
(a) and (b), the dissociation rate coefficient,
k
d
, is given by:
D
2
:
007
0
:
6065
k
d
¼ð
0
:
3678
þ
1
:
10262
Þ
ð
11
:
5b
Þ
fd
The fit is not good. Only three data points are available. The availability of more data points
would lead to a more reliable fit. The dissociation rate coefficient,
k
d
, for a single-fractal
analysis exhibits very close to a second (equal to 2.007) order of dependence on the fractal
dimension,
D
fd
, or the degree of heterogeneity that exists in the dissociation phase on the
biosensor surface.
Figure 11.11c
and
Table 11.6
(a) and (b) show the increase in the affinity,
K
(
k
/
k
d
), with an
increase in the ratio of the fractal dimensions in the binding and in the dissociation phases (
D
f
/
D
fd
), for a single-fractal analysis. For the data shown in
Figure 11.11a
and
Table 11.6
(a)
and (b), the affinity,
K
,isgivenby:
¼
1
:
746
0
:
978
K
ð¼
k
=
k
d
Þ¼ð
13
:
þ
:
Þð
D
f
=
D
fd
Þ
ð
:
Þ
6
124
34
11
5c
