Conformational study of melectin and antapin antimicrobial peptides in model membrane environments

0475296 - ÚOCHB 2018 RIV NL eng J - Článek v odborném periodiku
Kocourková, L. - Novotná, P. - Čujová, Sabína - Čeřovský, Václav - Urbanová, M. - Setnička, V.
Conformational study of melectin and antapin antimicrobial peptides in model membrane environments.
Spectrochimica Acta Part A-Molecular and Biomolecular Spectroscopy. Roč. 170, Jan 5 (2017), s. 247-255. ISSN 1386-1425. E-ISSN 1873-3557
Institucionální podpora: RVO:61388963
Klíčová slova: antimicrobial peptides * conformation * liposomes * model membranes * circular dichroism * infrared spectroscopy
Obor OECD: Analytical chemistry
Impakt faktor: 2.880, rok: 2017

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 alpha-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 alpha-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 alpha-helical conformation was lower, which corresponds with their moderate hemolytic activity.
Trvalý link: http://hdl.handle.net/11104/0272134