Fig. 4 | Communications Biology

Fig. 4

From: Structure-function-guided exploration of the antimicrobial peptide polybia-CP identifies activity determinants and generates synthetic therapeutic candidates

Fig. 4

Physicochemical features and structure of Pol-CP-NH2 and second-generation analogs. Circular dichroism spectra of the peptides at 50 µmol L−1 in water, MeOH/Water (1:1, v/v), PBS (pH 7.4), POPC (10 mmol L−1), POPC:DOPE (3:1, 10 mmol L−1), POPC:POPG (3:1, 10 mmol L−1), SDS (20 mmol L−1), TFE/Water (2:3, 3:2, 4:1, 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

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