Vibrational and electronic circular dichroism as powerful tools for the conformational analysis of cationic antimicrobial peptides

Antimicrobial and hemolytic activities of cationic α-helical antimicrobial peptides depend on their ability to adopt an amphipathic α-helical conformation on the cell membrane surface. Using vibrational and electronic circular dichroism, we carried out a conformational study of two α-helical antimicrobial peptides, melectin and antapin, in various environments mimicking bacterial and eukaryotic membranes. The results showed a significant difference in the content of α-helical conformation in the environment mimicking the bacterial and eukaryotic membranes. Graphical abstract