Interaction of Halictine-Related Antimicrobial Peptides with Membrane Models
Identifikátory výsledku
Kód výsledku v IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F19%3A00503943" target="_blank" >RIV/61388963:_____/19:00503943 - isvavai.cz</a>
Nalezeny alternativní kódy
RIV/00216208:11320/19:10400176
Výsledek na webu
<a href="https://www.mdpi.com/1422-0067/20/3/631/htm" target="_blank" >https://www.mdpi.com/1422-0067/20/3/631/htm</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.3390/ijms20030631" target="_blank" >10.3390/ijms20030631</a>
Alternativní jazyky
Jazyk výsledku
angličtina
Název v původním jazyce
Interaction of Halictine-Related Antimicrobial Peptides with Membrane Models
Popis výsledku v původním jazyce
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.
Název v anglickém jazyce
Interaction of Halictine-Related Antimicrobial Peptides with Membrane Models
Popis výsledku anglicky
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.
Klasifikace
Druh
J<sub>imp</sub> - Článek v periodiku v databázi Web of Science
CEP obor
—
OECD FORD obor
10610 - Biophysics
Návaznosti výsledku
Projekt
<a href="/cs/project/GAP208%2F10%2F0376" target="_blank" >GAP208/10/0376: Modelování interakce antibakteriálních peptidů s modelovou membránou a možnost predikce jejich biologické aktivity</a><br>
Návaznosti
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Ostatní
Rok uplatnění
2019
Kód důvěrnosti údajů
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Údaje specifické pro druh výsledku
Název periodika
International Journal of Molecular Sciences
ISSN
1422-0067
e-ISSN
—
Svazek periodika
20
Číslo periodika v rámci svazku
3
Stát vydavatele periodika
CH - Švýcarská konfederace
Počet stran výsledku
26
Strana od-do
631
Kód UT WoS článku
000462412500175
EID výsledku v databázi Scopus
2-s2.0-85061141875