Conformational study of melectin and antapin antimicrobial peptides in model membrane environments.
Antimicrobial peptides have long been considered as promising compounds against drug-resistant pathogens. In this work, we studied the secondary structure of antimicrobial peptides melectin and antapin using electronic (ECD) and vibrational circular dichroism (VCD) spectroscopies that are sensitive to peptide secondary structures. The results from quantitative ECD spectral evaluation by Dichroweb and CDNN program and from the qualitative evaluation of the VCD spectra were compared. The antimicrobial activity of the selected peptides depends on their ability to adopt an amphipathic α-helical conformation on the surface of the bacterial membrane. Hence, solutions of different zwitterionic and negatively charged liposomes and micelles were used to mimic the eukaryotic and bacterial biological membranes. The results show a significant content of α-helical conformation in the solutions of negatively charged liposomes mimicking the bacterial membrane, thus correlating with the antimicrobial activity of the studied peptides. On the other hand in the solutions of zwitterionic liposomes used as models of the eukaryotic membranes, the fraction of α-helical conformation was lower, which corresponds with their moderate hemolytic activity.
['Kocourková|Lucie|L|', 'Novotná|Pavlína|P|', 'Čujová|Sabína|S|', 'Čeřovský|Václav|V|', 'Urbanová|Marie|M|', 'Setnička|Vladimír|V|']
D023181:Antimicrobial Cationic Peptides D002462:Cell Membrane D002942:Circular Dichroism D017666:Deuterium Oxide D006461:Hemolysis D008051:Lipid Bilayers D008081:Liposomes D008823:Micelles D008826:Microbial Sensitivity Tests D011487:Protein Conformation D012967:Sodium Dodecyl Sulfate D012996:Solutions
Conformation Antimicrobial peptides Model membranes Circular dichroism Liposomes Infrared spectroscopy