Počet záznamů: 1
Interaction of Halictine-Related Antimicrobial Peptides with Membrane Models
- 1.0503943 - ÚOCHB 2020 RIV CH eng J - Článek v odborném periodiku
Pazderková, Markéta - Maloň, P. - Zíma, V. - Hofbauerová, K. - Kopecký, V. Jr. - Kočišová, E. - Pazderka, T. - Čeřovský, Václav - Bednárová, Lucie
Interaction of Halictine-Related Antimicrobial Peptides with Membrane Models.
International Journal of Molecular Sciences. Roč. 20, č. 3 (2019), č. článku 631. E-ISSN 1422-0067
Grant CEP: GA ČR GAP208/10/0376
Institucionální podpora: RVO:61388963
Klíčová slova: antibacterial peptides * halictine * circular dichroism * fluorescence * infrared spectroscopy
Obor OECD: Biophysics
Impakt faktor: 4.556, rok: 2019
Způsob publikování: Open access
https://www.mdpi.com/1422-0067/20/3/631/htm
We have investigated structural changes of peptides related to antimicrobial peptide Halictine-1 (HAL-1) induced by interaction with various membrane-mimicking models with the aim to identify a mechanism of the peptide mode of action and to find a correlation between changes of primary/secondary structure and biological activity. Modifications in the HAL-1 amino acid sequence at particular positions, causing an increase of amphipathicity (Arg/Lys exchange), restricted mobility (insertion of Pro) and consequent changes in antimicrobial and hemolytic activity, led to different behavior towards model membranes. Secondary structure changes induced by peptide-membrane interaction were studied by circular dichroism, infrared spectroscopy, and fluorescence spectroscopy. The experimental results were complemented by molecular dynamics calculations. Anhelical structure has been found to be necessary but not completely sufficient for the HAL-1 peptides antimicrobial action. The role of alternative conformations (such assheet, PPII or 3(10)-helix) also seems to be important. A mechanism of the peptide mode of action probably involves formation of peptide assemblies (possibly membrane pores), which disrupt bacterial membrane and, consequently, allow membrane penetration.
Trvalý link: http://hdl.handle.net/11104/0296778
Počet záznamů: 1