Structural and dynamical surface properties of phosphatidylethanolamine containing membranes

The hydration of solid dimyristoylphosphatidylethanolamine (DMPE) produces a negligible shift in the asymmetric stretching frequency of the phosphate groups in contrast to dimyristoylphosphatidylcholine (DMPC). This suggests that the hydration of DMPE is not a consequence of the disruption of the so...

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Autor principal: Gordillo, Gabriel Jorge
Publicado: 2009
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Acceso en línea:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00052736_v1788_n5_p918_Bouchet
http://hdl.handle.net/20.500.12110/paper_00052736_v1788_n5_p918_Bouchet
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spelling paper:paper_00052736_v1788_n5_p918_Bouchet2023-06-08T14:29:50Z Structural and dynamical surface properties of phosphatidylethanolamine containing membranes Gordillo, Gabriel Jorge Cyclic voltammetry Dipole potential Interphase water activity Monolayer Phosphate asymmetric frequency Phosphatidylethanolamine Protein penetration ammonia dimyristoylphosphatidylcholine dimyristoylphosphatidylethanolamine ethanolamine derivative lipid long chain fatty acid coenzyme A ligase nitrogen phosphate phosphatidylcholine phosphatidylethanolamine phosphorus protein unclassified drug article cell disruption cell energy controlled study correlation analysis dipole electric field energy absorption gene translocation hydration interface pressure interphase membrane biology membrane structure molecular dynamics molecular interaction monolayer culture polarization priority journal surface property water content Adsorption Animals Biophysical Phenomena Lecithins Membrane Lipids Membrane Potentials Membranes, Artificial Micelles Molecular Structure Phosphatidylethanolamines Pressure Proteins Spectroscopy, Fourier Transform Infrared Surface Properties Thermodynamics The hydration of solid dimyristoylphosphatidylethanolamine (DMPE) produces a negligible shift in the asymmetric stretching frequency of the phosphate groups in contrast to dimyristoylphosphatidylcholine (DMPC). This suggests that the hydration of DMPE is not a consequence of the disruption of the solid lattice of the phosphate groups as occurs in DMPC. The strong lateral interactions between NH3 and PO2 - groups present in the solid PEs remain when the lipids are fully hydrated and seem to be a limiting factor for the hydration of the phosphate group hindering the reorientation of the polar heads. The lower mobility is reflected in a higher energy to translocate the phosphoethanolamine (P-N) dipoles in an electrical field. This energy is decreased in the presence of increasing ratios of PCs of saturated chains in phosphoethanolamine monolayer. The association of PC and PE in the membrane affecting the reorientation of the P-N groups is dependent of the chain-chain interaction. The dipole potentials of PCs and PEs mixtures show different behaviors according to the saturation of the acyl chain. This was correlated with the area in monolayers and the hydration of the P-N groups. In spite of the low hydration, DMPE is still able to adsorb fully hydrated proteins, although in a lower rate than DMPC at the same surface pressure. This indicates that PE interfaces posses an excess of surface free energy to drive protein interaction. The relation of this free energy with the low water content is discussed. © 2009 Elsevier B.V. All rights reserved. Fil:Gordillo, G. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 2009 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00052736_v1788_n5_p918_Bouchet http://hdl.handle.net/20.500.12110/paper_00052736_v1788_n5_p918_Bouchet
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic Cyclic voltammetry
Dipole potential
Interphase water activity
Monolayer
Phosphate asymmetric frequency
Phosphatidylethanolamine
Protein penetration
ammonia
dimyristoylphosphatidylcholine
dimyristoylphosphatidylethanolamine
ethanolamine derivative
lipid
long chain fatty acid coenzyme A ligase
nitrogen
phosphate
phosphatidylcholine
phosphatidylethanolamine
phosphorus
protein
unclassified drug
article
cell disruption
cell energy
controlled study
correlation analysis
dipole
electric field
energy absorption
gene translocation
hydration
interface pressure
interphase
membrane biology
membrane structure
molecular dynamics
molecular interaction
monolayer culture
polarization
priority journal
surface property
water content
Adsorption
Animals
Biophysical Phenomena
Lecithins
Membrane Lipids
Membrane Potentials
Membranes, Artificial
Micelles
Molecular Structure
Phosphatidylethanolamines
Pressure
Proteins
Spectroscopy, Fourier Transform Infrared
Surface Properties
Thermodynamics
spellingShingle Cyclic voltammetry
Dipole potential
Interphase water activity
Monolayer
Phosphate asymmetric frequency
Phosphatidylethanolamine
Protein penetration
ammonia
dimyristoylphosphatidylcholine
dimyristoylphosphatidylethanolamine
ethanolamine derivative
lipid
long chain fatty acid coenzyme A ligase
nitrogen
phosphate
phosphatidylcholine
phosphatidylethanolamine
phosphorus
protein
unclassified drug
article
cell disruption
cell energy
controlled study
correlation analysis
dipole
electric field
energy absorption
gene translocation
hydration
interface pressure
interphase
membrane biology
membrane structure
molecular dynamics
molecular interaction
monolayer culture
polarization
priority journal
surface property
water content
Adsorption
Animals
Biophysical Phenomena
Lecithins
Membrane Lipids
Membrane Potentials
Membranes, Artificial
Micelles
Molecular Structure
Phosphatidylethanolamines
Pressure
Proteins
Spectroscopy, Fourier Transform Infrared
Surface Properties
Thermodynamics
Gordillo, Gabriel Jorge
Structural and dynamical surface properties of phosphatidylethanolamine containing membranes
topic_facet Cyclic voltammetry
Dipole potential
Interphase water activity
Monolayer
Phosphate asymmetric frequency
Phosphatidylethanolamine
Protein penetration
ammonia
dimyristoylphosphatidylcholine
dimyristoylphosphatidylethanolamine
ethanolamine derivative
lipid
long chain fatty acid coenzyme A ligase
nitrogen
phosphate
phosphatidylcholine
phosphatidylethanolamine
phosphorus
protein
unclassified drug
article
cell disruption
cell energy
controlled study
correlation analysis
dipole
electric field
energy absorption
gene translocation
hydration
interface pressure
interphase
membrane biology
membrane structure
molecular dynamics
molecular interaction
monolayer culture
polarization
priority journal
surface property
water content
Adsorption
Animals
Biophysical Phenomena
Lecithins
Membrane Lipids
Membrane Potentials
Membranes, Artificial
Micelles
Molecular Structure
Phosphatidylethanolamines
Pressure
Proteins
Spectroscopy, Fourier Transform Infrared
Surface Properties
Thermodynamics
description The hydration of solid dimyristoylphosphatidylethanolamine (DMPE) produces a negligible shift in the asymmetric stretching frequency of the phosphate groups in contrast to dimyristoylphosphatidylcholine (DMPC). This suggests that the hydration of DMPE is not a consequence of the disruption of the solid lattice of the phosphate groups as occurs in DMPC. The strong lateral interactions between NH3 and PO2 - groups present in the solid PEs remain when the lipids are fully hydrated and seem to be a limiting factor for the hydration of the phosphate group hindering the reorientation of the polar heads. The lower mobility is reflected in a higher energy to translocate the phosphoethanolamine (P-N) dipoles in an electrical field. This energy is decreased in the presence of increasing ratios of PCs of saturated chains in phosphoethanolamine monolayer. The association of PC and PE in the membrane affecting the reorientation of the P-N groups is dependent of the chain-chain interaction. The dipole potentials of PCs and PEs mixtures show different behaviors according to the saturation of the acyl chain. This was correlated with the area in monolayers and the hydration of the P-N groups. In spite of the low hydration, DMPE is still able to adsorb fully hydrated proteins, although in a lower rate than DMPC at the same surface pressure. This indicates that PE interfaces posses an excess of surface free energy to drive protein interaction. The relation of this free energy with the low water content is discussed. © 2009 Elsevier B.V. All rights reserved.
author Gordillo, Gabriel Jorge
author_facet Gordillo, Gabriel Jorge
author_sort Gordillo, Gabriel Jorge
title Structural and dynamical surface properties of phosphatidylethanolamine containing membranes
title_short Structural and dynamical surface properties of phosphatidylethanolamine containing membranes
title_full Structural and dynamical surface properties of phosphatidylethanolamine containing membranes
title_fullStr Structural and dynamical surface properties of phosphatidylethanolamine containing membranes
title_full_unstemmed Structural and dynamical surface properties of phosphatidylethanolamine containing membranes
title_sort structural and dynamical surface properties of phosphatidylethanolamine containing membranes
publishDate 2009
url https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00052736_v1788_n5_p918_Bouchet
http://hdl.handle.net/20.500.12110/paper_00052736_v1788_n5_p918_Bouchet
work_keys_str_mv AT gordillogabrieljorge structuralanddynamicalsurfacepropertiesofphosphatidylethanolaminecontainingmembranes
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