Formation of arenicin-1 microdomains in bilayers and their specific lipid interaction revealed by Z-scan FCS
Language English Country Germany Media print-electronic
Document type Evaluation Study, Journal Article, Research Support, Non-U.S. Gov't
- MeSH
- Models, Biological MeSH
- Diffusion MeSH
- Spectrometry, Fluorescence methods MeSH
- Antimicrobial Cationic Peptides chemistry metabolism MeSH
- Lipid Bilayers chemistry metabolism MeSH
- Lipids chemistry MeSH
- Publication type
- Journal Article MeSH
- Evaluation Study MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Antimicrobial Cationic Peptides MeSH
- Lipid Bilayers MeSH
- Lipids MeSH
Z-scan fluorescence correlation spectroscopy (FCS) is employed to characterize the interaction between arenicin-1 and supported lipid bilayers (SLBs) of different compositions. Lipid analogue C8-BODIPY 500/510C5-HPC and ATTO 465 labelled arenicin-1 are used to detect changes in lipid and peptide diffusion upon addition of unlabelled arenicin-1 to SLBs. Arenicin-1 decreases lipid mobility in negatively charged SLBs. According to diffusion law analysis, microdomains of significantly lower lipid mobility are formed. The analysis of peptide FCS data confirms the presence of microdomains for anionic SLBs. No indications of microdomain formation are detected in SLBs composed purely of zwitterionic lipids. Additionally, our FCS results imply that arenicin-1 exists in the form of oligomers and/or aggregates when interacting with membranes of both compositions.
References provided by Crossref.org
Fluorescence Lifetime Correlation Spectroscopy (FLCS): concepts, applications and outlook
