Biology Reference
In-Depth Information
Table 11.1.
A partial list of reported dynamic force spectroscopy studies of leukocyte
selectins and integrins
Ligand-receptor
pair
Approach
Rupture force
(pN)
Intrinsic
lifetime,
τ
0
(s)
Potential
width,
γ
(Å)
References
Selectin-ligand:
P-selectin/PSGL-1
(1)
110-170
50
2.5
91
P-selectin/PSGL-1
(3)
30-220
5
1.4
92
P-selectin/sLeX
(1)
20-220
3
0.8, 4.5
62
E-selectin/sLeX
(1)
40-160
3
0.9, 5
62
L-selectin/sLeX
(1)
20-140
0.2
0.8, 4.5
62
Integrin-ligand:
A
L
B
2
/ICAM-1
(2)(4)
20-320
6
0.24, 2.1
5
A
L
B
2
/ICAM-1
(2)
50-300
50
0.31, 4.5
6
A
M
B
2
/ICAM-1
(3)
50-200
4
1.8
97
A
4
B
1
/VCAM-1
(1)(2)
15-130
25
1, 5.5
37
A
5
B
1
/ibronectin
(1)
40-170
83
0.9, 4
33
A
5
B
1
/GRGDSP
(1)
32 ± 2
N/A
31
A
2
B
1
/collagen (2) 40-100 0.8 2.3 98
Notes:
Experimental Approaches: (1) Protein on tip and substrate, (2) Cell
attached on cantilever and protein on substrate, (3) Cell on substrate and
proteins on tip, (4) Cells on substrate and tip; for integrins with different
activation states, only the lifetime for the high afinity state was included.
11.5 CONCLUSIONS AND FUTURE DIRECTIONS
We have shown that the AFM is a well-established tool to probe the adhesion
strength of biomolecular interactions. Unlike bulk studies, such as surface
plasmon resonance, that provide averaged lifetimes and energies, AFM allows
us to detect alternative dissociation pathways with possible intermediate
states at the single-molecule level. Moreover, the AFM and other force
Search WWH ::
Custom Search