TABLE 2.
The interaction of TH-(1–43), THp-(1–43), and 14-3-3 proteins with liposomes of different composition as measured by SPR
| Ligand | S0.5a for the binding to liposomes made of |
||
|---|---|---|---|
| PC:PBPS (1:1) | PC:DOPG (1:1) | PC:PBPS:SDPS:DPPC | |
| μm | |||
| TH-(1–43) | 38 ± 4 | 58 ± 10 | 24.5 ± 1.5 |
| THp-(1–43) | 144 ± 19 | 474 ± 13 | 135 ± 15 |
| 14-3-3ζ | 10 ± 0.5 | 21 ± 3.8 | 5 ± 0.1b |
| 14-3-3η | 13 ± 1.7 | 20 ± 2.4 | —b |
| 14-3-3γ | 1.9 ± 0.1c | 8.7 ± 0.4c | 1.3 ± 0.5c |
| 14-3-3γ·THp-(1–43) (1:2) | 1.3 ± 0.2 | —b | 0.64 ± 0.1 |
a S0.5, concentration of peptides, 14-3-3 proteins, or 14-3-3γ·THp-(1–43) complex for half-maximal binding, obtained from binding isotherms (Fig. 3).
b Not measured.
c The S0.5 values for 14-3-3γ are significantly different for the values obtained for 14-3-3ζ and -η isoforms with the three liposome compositions (analysis of variance; p < 0.005).