Table 1.
Analog | Breaking Point |
2nd Minimum |
1st Minimum |
n | |||
---|---|---|---|---|---|---|---|
A (Å2) | π (mN/m) | Cs−1 (mN/m) | π (mN/m) | Cs−1 (mN/m) | π (mN/m) | ||
Control | 66.0 ± 2.9 | 41.7 ± 2.9 | – | – | – | – | 9 |
WT | 89.8 ± 4.1 | 38.7 ± 0.9 | 14.3 ± 2.6 | 39.5 ± 0.5 | 32.2 ± 4.0 | 26.1 ± 1.5 | 10 |
K8E | 51.7 ± 3.2 | 43.7 ± 0.9 | 13.7 ± 2.3 | 36.9 ± 0.9 | 21.3 ± 2.2 | 30.8 ± 1.1 | 8 |
K15E | 52.3 ± 2.2 | 43.7 ± 0.2 | 21.8 ± 1.2 | 40.5 ± 0.6 | 19.7 ± 1.0 | 26.4 ± 0.3 | 4 |
K25E | 59.8 ± 1.8 | 47.1 ± 0.6 | – | – | 22.2 ± 1.5 | 29.3 ± 1.7 | 8 |
K28E | 56.7 ± 7.2 | 43.8 ± 1.4 | 13.3 ± 2.5 | 35.5 ± 1.0 | 20.5 ± 1.4 | 28.8 ± 0.7 | 4 |
Breaking point of isotherms signifies the change of slope, which in case of WT shows the early onset of peptide expulsion. For all other analogs an obvious isotherm flattening was associated with collapse. The position of the second minimum of the inverse compressibility parameter Cs2−1 reflects “softening” of the monolayer associated with pressure-dependent redistribution of the peptide to a shallower position. The second minima are low for the active peptides, but are either higher for the compromised peptides (K15E), or may not even exist (K25E). The first Cs1−1 minimum presumably reflects compaction and ordering of the peptides within the still expanded monolayer and its position shows no direct correlation with activity. The number of experiments is shown in the last column (n).