Intragenic antimicrobial peptides (IAPs) from human proteins with potent antimicrobial and anti-inflammatory activity
Fig 2
Hs IAPs transition to α-helical structure upon interaction with model phospholipid membranes and induce disturbances in the P´β→Lα phase transition of vesicles.
a. Far-UV CD scans were performed to evaluate the secondary structure of Hs IAPs in buffer alone (40 μM solution peptide in phosphate buffer), represented as a black line, and after the addition of 2 mM DMPC, represented as a red line, or in the presence of 2 mM 2:1 DMPC:DMPG, blue line. b. Heating thermal scans of DMPC and 2:1 DMPC:DMPG LUVs enriched with 4 mol% IAPs. Black line corresponds to experimental data. Red line corresponds to a non-two state model fitting with two components of the main phase transition of model vesicles. Hs IAPs and the corresponding LUV compositions are indicated in each inset of the figure.