TABLE 3.
LC4 peptide inhibition dissociation constants
The values shown for the random peptide (DNYEFDG) correspond to dissociation constants Ki and K′i, respectively, used to characterize the mixed inhibition exhibited by this peptide and is different from competitive inhibition displayed by LC4 and WASP peptides, which is characterized by a single dissociation constant Ki.
| Peptide | Ki | Ki′ |
|---|---|---|
| LC4 (165–171) | 17 ± 2 μm | |
| LC4 (165–171) W165A | 144 ± 7 μm | |
| LC4 (163–183) | 18 ± 2 μm | |
| LC4 (163–183) W165A | 130 ± 5 μm | |
| WASP (496–502) | 532 ± 33 μm | |
| DNYEFDG | 1,807 ± 258 μm | 1,821 ± 130 μm |