Fig. 3
Physicochemical features and structure of Pol-CP-NH2 and Ala-scan analogs. a Circular dichroism spectra of Pol-CP-NH2 and Ala-scan derivatives at 50 µmol L−1 in water, PBS (pH 7.4) and TFE/Water (3:2, v/v) showing peptides transition from unstructured in water to helically structured in TFE/water. Circular dichroism spectra were recorded after four accumulations at 20 oC, using a 1 mm path length quartz cell, between 260 and 190 nm at 50 nm min-1, with a bandwidth of 0.5 nm. b MIC (µmol L−1) average for each peptide against the first set of bacteria (E. coli BL21, P. aeruginosa PA01 and PA14, and S. aureus ATCC12600) in three independent replicates vs. fH in TFE/Water solution, where blue boxes represent peptides with lower activity and red boxes show peptides with higher activity compared to the wild-type. Optimal activity is reached in most of the cases for fH values higher than the wild-type
