Association of an acylated model peptide with DPPC-DPPS lipid membranes
Research output: Contribution to journal › Journal article › Research › peer-review
The interaction between a small positively charged peptide with a N-terminally linked acyl chain and dipalmitoylphosphatidylcholine-dipalmitoylphosphatidylserine (DPPC-DPPS) lipid membranes has been studied by means of fluorescence resonance energy transfer. Two different lipid compositions were used: a neutral membrane (100 mol% DPPC), and a negatively charged membrane (30 mol% DPPS in DPPC). The fluorescence resonance energy transfer results reveal that the peptide associates with both types of membranes. Furthermore, it is found that the slope of the titration curve for the negatively charged membranes is much steeper than that for the neutral membranes. This indicates a higher binding affinity of the acylated peptide towards negatively charged lipid membranes as compared with neutral lipid membranes.
|Journal||International Journal of Pharmaceutics|
|Number of pages||5|
|Publication status||Published - 19 Feb 2001|
- Acylated peptide, Fluorescence resonance energy transfer, Negatively charged membranes, Peptide-membrane association