Interaction of Halictine-Related Antimicrobial Peptides with Membrane Models.
Int J Mol Sci
; 20(3)2019 Feb 01.
Article
en En
| MEDLINE
| ID: mdl-30717183
ABSTRACT
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. An α-helical structure has been found to be necessary but not completely sufficient for the HAL-1 peptides antimicrobial action. The role of alternative conformations (such as ß-sheet, PPII or 310-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.
Palabras clave
Texto completo:
1
Banco de datos:
MEDLINE
Asunto principal:
Fosfatidilcolinas
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Fosfatidilgliceroles
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Péptidos Catiónicos Antimicrobianos
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Membrana Dobles de Lípidos
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Antibacterianos
Idioma:
En
Año:
2019
Tipo del documento:
Article