Biomedical Engineering Reference
In-Depth Information
Table 15.6: Binding and dissociation rate coefficients for the binding and dissociation phase for
different concentrations (in nM) of thrombin to best aptamer in generation 4 (G4.04422)
immobilized on a SA chip (Platt et al.,
2009a,b
).
Thrombin
Concentration in
Solution (nM)
k
k
d
D
f
D
fd
16
0.9997
0.00591
1.4477
0.0967
2.0416
0.0341
2.2498
0.0604
32
4.314
0.128
1.0428
0.0364
2.3586
0.01748
1.9400
0.0320
65
7.519
0.486
3.2895
0.107
2.4362
0.0371
2.2744
0.02982
130
18.714 0.348
6.0088 0.1082
2.6236 0.0109
2.3398 0.02874
rate coefficient
k
d
and the fractal dimension for dissociation
D
fd
for a single-fractal analysis
are given in
Table 15.6
. The affinity
K
(
¼
k
/
k
d
) value is 0.691.
Figure 15.9b
shows the binding of 32 nM thrombin in solution to aptamer (G4.04422; best
aptamer in generation 4) immobilized on a SA chip. A single-fractal analysis is adequate
to describe the binding and the dissociation kinetics. The values of (a) the binding rate coef-
ficient
k
and the fractal dimension
D
f
for a single-fractal analysis, and (b) the dissociation
rate coefficient
k
d
and the fractal dimension for dissociation
D
fd
for a single-fractal analysis
are given in
Table 15.6
. The affinity
K
(
¼
k
/
k
d
) value is 4.14.
Figure 15.9c
shows the binding of 65 nM thrombin in solution to aptamer (G4.04422; best
aptamer in generation 4) immobilized on a SA chip. A single-fractal analysis is adequate
to describe the binding and the dissociation kinetics. The values of (a) the binding rate coef-
ficient
k
and the fractal dimension
D
f
for a single-fractal analysis, and (b) the dissociation
rate coefficient
k
d
and the fractal dimension for dissociation
D
fd
for a single-fractal analysis
are given in
Table 15.6
. The affinity
K
(
¼
k
/
k
d
) value is 2.29.
Figure 15.9d
shows the binding of 130 nM thrombin in solution to aptamer (G4.04422; best
aptamer in generation 4) immobilized on a SA chip. A single-fractal analysis is adequate to
describe the binding and the dissociation kinetics. The values of (a) the binding rate coeffi-
cient
k
and the fractal dimension
D
f
for a single-fractal analysis, and (b) the dissociation rate
coefficient
k
d
and the fractal dimension for dissociation
D
fd
for a single-fractal analysis are
given in
Table 15.6
. The affinity
K
(
¼
k
/
k
d
) value is 3.11.
Figure 15.10a
and
Table 15.6
show the increase in the binding rate coefficient
k
with an
increase in the thrombin concentration in solution in the 16-130 nM range for binding to a
best aptamer in generation 4(G4.04422). For the data shown in
Figure 15.10a
, the binding
rate coefficient
k
is given by:
1
:
34
0
:
181
k
¼ð
0
:
030
0
:
010
Þ½
thrombin concentration, nM
ð
15
:
5a
Þ
