The hydrophobic acyl-chain effect in the lipid domains appearance through phospholipid bilayers

Liviu Movileanu; Dumitru Popescu; Maria Luiza Flonta

doi:10.1016/S0166-1280(98)00112-2

The hydrophobic acyl-chain effect in the lipid domains appearance through phospholipid bilayers

Liviu Movileanu, Dumitru Popescu, Maria Luiza Flonta

Research output: Contribution to journal › Article › peer-review

6 Scopus citations

Abstract

An intermolecular interaction model for selective association processes of double-chain phospholipids in bilayer lipid membranes has been proposed, analysed and solved numerically. A large variety of binary mixtures of asymmetrical double-chain phospholipids with the cross-sectional areas of the polar headgroups a₁ = 40 Å² (the first component) and a₂ = 60 Å² (the second component) have been investigated. Changing the hydrophobic acyl-chain lengths of both mixture components, we found in all cases that the self-association probability (the association of like-pairs of phospholipids) of the first component in parallel alignment of the electric dipole moments of the polar headgroups is higher than the cross-association probability (the association of cross-pairs of phospholipids) and the self-association probability of the second component. This result is in good agreement with the experimental evidence that where the cross-sectional area of the polar headgroups matches the hydrocarbon chain-packing cross-sectional area (a ≅ 2∑ ≅ 40 Å²), lipids possess a high tendency to aggregate into well packed bilayer structures with the acyl-chains oriented perpendicularly to the bilayer plane. Our theoretical data confirm that the double-chain phospholipids may associate themselves into anti-parallel alignment of the polar headgroups (P′₂₂) as well. The hydrophobic acyl-chain effect of phospholipids may modulate the distribution of lipid domains within bilayers that have a large variety of functional roles in cellular metabolism.

Original language	English (US)
Pages (from-to)	213-227
Number of pages	15
Journal	Journal of Molecular Structure: THEOCHEM
Volume	434
Issue number	1-3
DOIs	https://doi.org/10.1016/S0166-1280(98)00112-2
State	Published - Aug 4 1998
Externally published	Yes

Keywords

Bilayer lipid membrane
Computer simulation
Hydrophobic acyl-chain effect
Lipid domains
Phospholipid

ASJC Scopus subject areas

Biochemistry
Condensed Matter Physics
Physical and Theoretical Chemistry

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10.1016/S0166-1280(98)00112-2

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@article{ba422f27a4a84c02b9cc0507bbe8d9f5,

title = "The hydrophobic acyl-chain effect in the lipid domains appearance through phospholipid bilayers",

abstract = "An intermolecular interaction model for selective association processes of double-chain phospholipids in bilayer lipid membranes has been proposed, analysed and solved numerically. A large variety of binary mixtures of asymmetrical double-chain phospholipids with the cross-sectional areas of the polar headgroups a1 = 40 {\AA}2 (the first component) and a2 = 60 {\AA}2 (the second component) have been investigated. Changing the hydrophobic acyl-chain lengths of both mixture components, we found in all cases that the self-association probability (the association of like-pairs of phospholipids) of the first component in parallel alignment of the electric dipole moments of the polar headgroups is higher than the cross-association probability (the association of cross-pairs of phospholipids) and the self-association probability of the second component. This result is in good agreement with the experimental evidence that where the cross-sectional area of the polar headgroups matches the hydrocarbon chain-packing cross-sectional area (a ≅ 2∑ ≅ 40 {\AA}2), lipids possess a high tendency to aggregate into well packed bilayer structures with the acyl-chains oriented perpendicularly to the bilayer plane. Our theoretical data confirm that the double-chain phospholipids may associate themselves into anti-parallel alignment of the polar headgroups (P′22) as well. The hydrophobic acyl-chain effect of phospholipids may modulate the distribution of lipid domains within bilayers that have a large variety of functional roles in cellular metabolism.",

keywords = "Bilayer lipid membrane, Computer simulation, Hydrophobic acyl-chain effect, Lipid domains, Phospholipid",

author = "Liviu Movileanu and Dumitru Popescu and Flonta, {Maria Luiza}",

note = "Funding Information: We would like to express our thanks to Drs. J.M. Seddon, M. Wortis, M. Glaser, G.J. Gompper, J.B. Sorenssen, P. Mattjus and G. Victor for many fruitful discussions. We also convey thanks to the SOROS Foundation for financial support. We are very indebted to Dr. Gordon Reid for his expertise in checking the English and also to an anonymous referee for helpful suggestions to the manuscript.",

year = "1998",

month = aug,

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doi = "10.1016/S0166-1280(98)00112-2",

language = "English (US)",

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pages = "213--227",

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T1 - The hydrophobic acyl-chain effect in the lipid domains appearance through phospholipid bilayers

AU - Movileanu, Liviu

AU - Popescu, Dumitru

AU - Flonta, Maria Luiza

N1 - Funding Information: We would like to express our thanks to Drs. J.M. Seddon, M. Wortis, M. Glaser, G.J. Gompper, J.B. Sorenssen, P. Mattjus and G. Victor for many fruitful discussions. We also convey thanks to the SOROS Foundation for financial support. We are very indebted to Dr. Gordon Reid for his expertise in checking the English and also to an anonymous referee for helpful suggestions to the manuscript.

PY - 1998/8/4

Y1 - 1998/8/4

N2 - An intermolecular interaction model for selective association processes of double-chain phospholipids in bilayer lipid membranes has been proposed, analysed and solved numerically. A large variety of binary mixtures of asymmetrical double-chain phospholipids with the cross-sectional areas of the polar headgroups a1 = 40 Å2 (the first component) and a2 = 60 Å2 (the second component) have been investigated. Changing the hydrophobic acyl-chain lengths of both mixture components, we found in all cases that the self-association probability (the association of like-pairs of phospholipids) of the first component in parallel alignment of the electric dipole moments of the polar headgroups is higher than the cross-association probability (the association of cross-pairs of phospholipids) and the self-association probability of the second component. This result is in good agreement with the experimental evidence that where the cross-sectional area of the polar headgroups matches the hydrocarbon chain-packing cross-sectional area (a ≅ 2∑ ≅ 40 Å2), lipids possess a high tendency to aggregate into well packed bilayer structures with the acyl-chains oriented perpendicularly to the bilayer plane. Our theoretical data confirm that the double-chain phospholipids may associate themselves into anti-parallel alignment of the polar headgroups (P′22) as well. The hydrophobic acyl-chain effect of phospholipids may modulate the distribution of lipid domains within bilayers that have a large variety of functional roles in cellular metabolism.

AB - An intermolecular interaction model for selective association processes of double-chain phospholipids in bilayer lipid membranes has been proposed, analysed and solved numerically. A large variety of binary mixtures of asymmetrical double-chain phospholipids with the cross-sectional areas of the polar headgroups a1 = 40 Å2 (the first component) and a2 = 60 Å2 (the second component) have been investigated. Changing the hydrophobic acyl-chain lengths of both mixture components, we found in all cases that the self-association probability (the association of like-pairs of phospholipids) of the first component in parallel alignment of the electric dipole moments of the polar headgroups is higher than the cross-association probability (the association of cross-pairs of phospholipids) and the self-association probability of the second component. This result is in good agreement with the experimental evidence that where the cross-sectional area of the polar headgroups matches the hydrocarbon chain-packing cross-sectional area (a ≅ 2∑ ≅ 40 Å2), lipids possess a high tendency to aggregate into well packed bilayer structures with the acyl-chains oriented perpendicularly to the bilayer plane. Our theoretical data confirm that the double-chain phospholipids may associate themselves into anti-parallel alignment of the polar headgroups (P′22) as well. The hydrophobic acyl-chain effect of phospholipids may modulate the distribution of lipid domains within bilayers that have a large variety of functional roles in cellular metabolism.

KW - Bilayer lipid membrane

KW - Computer simulation

KW - Hydrophobic acyl-chain effect

KW - Lipid domains

KW - Phospholipid

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U2 - 10.1016/S0166-1280(98)00112-2

DO - 10.1016/S0166-1280(98)00112-2

M3 - Article

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SN - 0166-1280

VL - 434

SP - 213

EP - 227

JO - Journal of Molecular Structure: THEOCHEM

JF - Journal of Molecular Structure: THEOCHEM

IS - 1-3

ER -

The hydrophobic acyl-chain effect in the lipid domains appearance through phospholipid bilayers

Abstract

Keywords

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