Table 1.
Equilibrium constants for hemin binding to Aβ40.
| Complex a | log K1 | log K2 b | log β2 |
|---|---|---|---|
| [hemin(Aβ40)2] | 6.08 ± 0.02 | 4.77 | 10.84 ± 0.02 |
| [hemin(Aβ40)2] c | 5.60 ± 0.01 | 4.20 | 9.80 ± 0.01 |
| [hemin(Aβ40)2] d | 4.76 ± 0.03 | 4.30 | 9.05 ± 0.01 |
| [hemin(Aβ40)2] e | 5.30 ± 0.02 | 4.47 | 9.77 ± 0.04 |
| [hemin(Aβ40)2] f | 7.30 ± 0.02 | 4.02 | 11.32 ± 0.16 |
| [hemin(Aβ16)2] g | 4.80 ± 0.02 | 4.03 | 8.82 ± 0.02 |
a Standard conditions: hemin (5 μM) in pH 7.4 phosphate buffer (5 mM) at 23 °C. b Obtained as the difference between log β2 and log K1. c pH 6.89. d pH 6.3. e 50 mM phosphate buffer pH 7.4. f 37 °C. g 50 mM PBS, pH 7.5, 27 °C; [13].