Interaction of Halictine-Related Antimicrobial Peptides with Membrane Models

Result code in 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>
Alternative codes found
RIV/00216208:11320/19:10400176
Result on the web
<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>

Result language
angličtina
Original language name
Interaction of Halictine-Related Antimicrobial Peptides with Membrane Models
Original language description
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.
Czech name
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Czech description
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Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
—
OECD FORD branch
10610 - Biophysics

Project
<a href="/en/project/GAP208%2F10%2F0376" target="_blank" >GAP208/10/0376: Interaction of antibacterial peptides with the model membranes and possibility of the prediction of their biological activity</a><br>
Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year
2019
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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