Table 2.
Inhibitory constants of the studied of α- and β-fluorinated aminophosphonic acid sodium salts towards bovine cathepsin C.
| Dipeptide |
![]() 9 KI ± SD [mM] |
![]() 11 KI ± SD [mM] |
|
| ||
| Phe-Ala (a) -CH3 |
0.603 ± 0.1 | 0.733 ± 0.087 |
| Phe-Val (b) -CH(CH3)2 |
0.0951 ± 0.05 | 1.869 ± 0.171 |
| Phe-Leu (c) -CH2CH(CH3)2 |
0.309 ± 0.066 | 0.847 ± 0.38 |
| Phe-Ile (d) -CH(CH3)CH2CH3 |
0.273 ± 0.15 | up to a concentration of 0.37 mM, it does not inhibit activity; at a higher concentration, it precipitates |
| Phe-Phe (e) -CH2Ph |
precipitates in a buffer | precipitates in buffer |

