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Association of an acylated model peptide with DPPC-DPPS lipid membranes

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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.

OriginalsprogEngelsk
TidsskriftInternational Journal of Pharmaceutics
Vol/bind214
Udgave nummer1-2
Sider (fra-til)77-81
Antal sider5
ISSN0378-5173
DOI
StatusUdgivet - 19 feb. 2001

ID: 230987611