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

Tina B. Pedersen; Mads C. Sabra; Sven Frokjaer; Ole G. Mouritsen; Kent Jørgensen

doi:10.1016/S0378-5173(00)00636-0

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

Tina B. Pedersen, Mads C. Sabra, Sven Frokjaer, Ole G. Mouritsen, Kent Jørgensen^*

^*Corresponding author for this work

6 Citations (Scopus)

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.

Original language	English
Journal	International Journal of Pharmaceutics
Volume	214
Issue number	1-2
Pages (from-to)	77-81
Number of pages	5
ISSN	0378-5173
DOIs	https://doi.org/10.1016/S0378-5173(00)00636-0
Publication status	Published - 19 Feb 2001

Keywords

Acylated peptide
Fluorescence resonance energy transfer
Negatively charged membranes
Peptide-membrane association

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10.1016/S0378-5173(00)00636-0

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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",

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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

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U2 - 10.1016/S0378-5173(00)00636-0

DO - 10.1016/S0378-5173(00)00636-0

M3 - Journal article

C2 - 11282241

AN - SCOPUS:0035910869

SN - 0378-5173

VL - 214

SP - 77

EP - 81

JO - International Journal of Pharmaceutics

JF - International Journal of Pharmaceutics

IS - 1-2

ER -

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

Abstract

Keywords

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