Association of an acylated model peptide with DPPC-DPPS lipid membranes
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Association of an acylated model peptide with DPPC-DPPS lipid membranes. / Pedersen, Tina B.; Sabra, Mads C.; Frokjaer, Sven; Mouritsen, Ole G.; Jørgensen, Kent.
In: International Journal of Pharmaceutics, Vol. 214, No. 1-2, 19.02.2001, p. 77-81.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - Association of an acylated model peptide with DPPC-DPPS lipid membranes
AU - Pedersen, Tina B.
AU - Sabra, Mads C.
AU - Frokjaer, Sven
AU - Mouritsen, Ole G.
AU - Jørgensen, Kent
PY - 2001/2/19
Y1 - 2001/2/19
N2 - 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.
AB - 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.
KW - Acylated peptide
KW - Fluorescence resonance energy transfer
KW - Negatively charged membranes
KW - Peptide-membrane association
UR - http://www.scopus.com/inward/record.url?scp=0035910869&partnerID=8YFLogxK
U2 - 10.1016/S0378-5173(00)00636-0
DO - 10.1016/S0378-5173(00)00636-0
M3 - Journal article
C2 - 11282241
AN - SCOPUS:0035910869
VL - 214
SP - 77
EP - 81
JO - International Journal of Pharmaceutics
JF - International Journal of Pharmaceutics
SN - 0378-5173
IS - 1-2
ER -
ID: 230987611