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

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

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

Harvard

Pedersen, TB, Sabra, MC, Frokjaer, S, Mouritsen, OG & Jørgensen, K 2001, 'Association of an acylated model peptide with DPPC-DPPS lipid membranes', International Journal of Pharmaceutics, vol. 214, no. 1-2, pp. 77-81. https://doi.org/10.1016/S0378-5173(00)00636-0

APA

Pedersen, T. B., Sabra, M. C., Frokjaer, S., Mouritsen, O. G., & Jørgensen, K. (2001). Association of an acylated model peptide with DPPC-DPPS lipid membranes. International Journal of Pharmaceutics, 214(1-2), 77-81. https://doi.org/10.1016/S0378-5173(00)00636-0

Vancouver

Pedersen TB, Sabra MC, Frokjaer S, Mouritsen OG, Jørgensen K. Association of an acylated model peptide with DPPC-DPPS lipid membranes. International Journal of Pharmaceutics. 2001 Feb 19;214(1-2):77-81. https://doi.org/10.1016/S0378-5173(00)00636-0

Author

Pedersen, Tina B. ; Sabra, Mads C. ; Frokjaer, Sven ; Mouritsen, Ole G. ; Jørgensen, Kent. / Association of an acylated model peptide with DPPC-DPPS lipid membranes. In: International Journal of Pharmaceutics. 2001 ; Vol. 214, No. 1-2. pp. 77-81.

Bibtex

@article{38c67d833e0242edaf0e2b005f6d244d,
title = "Association of an acylated model peptide with DPPC-DPPS lipid membranes",
abstract = "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.",
keywords = "Acylated peptide, Fluorescence resonance energy transfer, Negatively charged membranes, Peptide-membrane association",
author = "Pedersen, {Tina B.} and Sabra, {Mads C.} and Sven Frokjaer and Mouritsen, {Ole G.} and Kent J{\o}rgensen",
year = "2001",
month = feb,
day = "19",
doi = "10.1016/S0378-5173(00)00636-0",
language = "English",
volume = "214",
pages = "77--81",
journal = "International Journal of Pharmaceutics",
issn = "0378-5173",
publisher = "Elsevier",
number = "1-2",

}

RIS

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