X-ray structure, thermodynamics, elastic properties and MD simulations of cardiolipin/dimyristoylphosphatidylcholine mixed membranes.
Identifieur interne : 000771 ( Main/Exploration ); précédent : 000770; suivant : 000772X-ray structure, thermodynamics, elastic properties and MD simulations of cardiolipin/dimyristoylphosphatidylcholine mixed membranes.
Auteurs : Alexander L. Boscia [États-Unis] ; Bradley W. Treece [États-Unis] ; Dariush Mohammadyani [États-Unis] ; Judith Klein-Seetharaman [Royaume-Uni] ; Anthony R. Braun [États-Unis] ; Tsjerk A. Wassenaar [Pays-Bas] ; Beate Klösgen [Danemark] ; Stephanie Tristram-Nagle [États-Unis]Source :
- Chemistry and physics of lipids [ 1873-2941 ] ; 2014.
Descripteurs français
- KwdFr :
- Calorimétrie différentielle à balayage, Cardiolipides (), Conformation moléculaire, Cristallographie aux rayons X, Dimyristoylphosphatidylcholine (), Dimyristoylphosphatidylcholine (métabolisme), Double couche lipidique (), Double couche lipidique (métabolisme), Gels (), Simulation de dynamique moléculaire, Température de transition, Thermodynamique.
- MESH :
- métabolisme : Dimyristoylphosphatidylcholine, Double couche lipidique.
- Calorimétrie différentielle à balayage, Cardiolipides, Conformation moléculaire, Cristallographie aux rayons X, Dimyristoylphosphatidylcholine, Double couche lipidique, Gels, Simulation de dynamique moléculaire, Température de transition, Thermodynamique.
English descriptors
- KwdEn :
- Calorimetry, Differential Scanning, Cardiolipins (chemistry), Crystallography, X-Ray, Dimyristoylphosphatidylcholine (chemistry), Dimyristoylphosphatidylcholine (metabolism), Gels (chemistry), Lipid Bilayers (chemistry), Lipid Bilayers (metabolism), Molecular Conformation, Molecular Dynamics Simulation, Thermodynamics, Transition Temperature.
- MESH :
- chemical , chemistry : Cardiolipins, Dimyristoylphosphatidylcholine, Gels, Lipid Bilayers.
- chemical , metabolism : Dimyristoylphosphatidylcholine, Lipid Bilayers.
- Calorimetry, Differential Scanning, Crystallography, X-Ray, Molecular Conformation, Molecular Dynamics Simulation, Thermodynamics, Transition Temperature.
Abstract
Cardiolipins (CLs) are important biologically for their unique role in biomembranes that couple phosphorylation and electron transport like bacterial plasma membranes, chromatophores, chloroplasts and mitochondria. CLs are often tightly coupled to proteins involved in oxidative phosphorylation. The first step in understanding the interaction of CL with proteins is to obtain the pure CL structure, and the structure of mixtures of CL with other lipids. In this work we use a variety of techniques to characterize the fluid phase structure, material properties and thermodynamics of mixtures of dimyristoylphosphatidylcholine (DMPC) with tetramyristoylcardiolipin (TMCL), both with 14-carbon chains, at several mole percentages. X-ray diffuse scattering was used to determine structure, including bilayer thickness and area/lipid, the bending modulus, KC, and SXray, a measure of chain orientational order. Our results reveal that TMCL thickens DMPC bilayers at all mole percentages, with a total increase of ∼6 Å in pure TMCL, and increases AL from 64 Å(2) (DMPC at 35 °C) to 109 Å(2) (TMCL at 50 °C). KC increases by ∼50%, indicating that TMCL stiffens DMPC membranes. TMCL also orders DMPC chains by a factor of ∼2 for pure TMCL. Coarse grain molecular dynamics simulations confirm the experimental thickening of 2 Å for 20mol% TMCL and locate the TMCL headgroups near the glycerol-carbonyl region of DMPC; i.e., they are sequestered below the DMPC phosphocholine headgroup. Our results suggest that TMCL plays a role similar to cholesterol in that it thickens and stiffens DMPC membranes, orders chains, and is positioned under the umbrella of the PC headgroup. CL may be necessary for hydrophobic matching to inner mitochondrial membrane proteins. Differential scanning calorimetry, SXray and CGMD simulations all suggest that TMCL does not form domains within the DMPC bilayers. We also determined the gel phase structure of TMCL, which surprisingly displays diffuse X-ray scattering, like a fluid phase lipid. AL=40.8 Å(2) for the ½TMCL gel phase, smaller than the DMPC gel phase with AL=47.2 Å(2), but similar to AL of DLPE=41 Å(2), consistent with untilted chains in gel phase TMCL.
DOI: 10.1016/j.chemphyslip.2013.12.010
PubMed: 24378240
Affiliations:
- Danemark, Pays-Bas, Royaume-Uni, États-Unis
- Groningue (province), Minnesota, Pennsylvanie
- Groningue (ville), Pittsburgh
- Université Carnegie-Mellon, Université de Groningue, Université de Pittsburgh
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Le document en format XML
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<term>Crystallography, X-Ray</term>
<term>Dimyristoylphosphatidylcholine (chemistry)</term>
<term>Dimyristoylphosphatidylcholine (metabolism)</term>
<term>Gels (chemistry)</term>
<term>Lipid Bilayers (chemistry)</term>
<term>Lipid Bilayers (metabolism)</term>
<term>Molecular Conformation</term>
<term>Molecular Dynamics Simulation</term>
<term>Thermodynamics</term>
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<term>Conformation moléculaire</term>
<term>Cristallographie aux rayons X</term>
<term>Dimyristoylphosphatidylcholine ()</term>
<term>Dimyristoylphosphatidylcholine (métabolisme)</term>
<term>Double couche lipidique ()</term>
<term>Double couche lipidique (métabolisme)</term>
<term>Gels ()</term>
<term>Simulation de dynamique moléculaire</term>
<term>Température de transition</term>
<term>Thermodynamique</term>
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<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Cardiolipins</term>
<term>Dimyristoylphosphatidylcholine</term>
<term>Gels</term>
<term>Lipid Bilayers</term>
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<front><div type="abstract" xml:lang="en">Cardiolipins (CLs) are important biologically for their unique role in biomembranes that couple phosphorylation and electron transport like bacterial plasma membranes, chromatophores, chloroplasts and mitochondria. CLs are often tightly coupled to proteins involved in oxidative phosphorylation. The first step in understanding the interaction of CL with proteins is to obtain the pure CL structure, and the structure of mixtures of CL with other lipids. In this work we use a variety of techniques to characterize the fluid phase structure, material properties and thermodynamics of mixtures of dimyristoylphosphatidylcholine (DMPC) with tetramyristoylcardiolipin (TMCL), both with 14-carbon chains, at several mole percentages. X-ray diffuse scattering was used to determine structure, including bilayer thickness and area/lipid, the bending modulus, KC, and SXray, a measure of chain orientational order. Our results reveal that TMCL thickens DMPC bilayers at all mole percentages, with a total increase of ∼6 Å in pure TMCL, and increases AL from 64 Å(2) (DMPC at 35 °C) to 109 Å(2) (TMCL at 50 °C). KC increases by ∼50%, indicating that TMCL stiffens DMPC membranes. TMCL also orders DMPC chains by a factor of ∼2 for pure TMCL. Coarse grain molecular dynamics simulations confirm the experimental thickening of 2 Å for 20mol% TMCL and locate the TMCL headgroups near the glycerol-carbonyl region of DMPC; i.e., they are sequestered below the DMPC phosphocholine headgroup. Our results suggest that TMCL plays a role similar to cholesterol in that it thickens and stiffens DMPC membranes, orders chains, and is positioned under the umbrella of the PC headgroup. CL may be necessary for hydrophobic matching to inner mitochondrial membrane proteins. Differential scanning calorimetry, SXray and CGMD simulations all suggest that TMCL does not form domains within the DMPC bilayers. We also determined the gel phase structure of TMCL, which surprisingly displays diffuse X-ray scattering, like a fluid phase lipid. AL=40.8 Å(2) for the ½TMCL gel phase, smaller than the DMPC gel phase with AL=47.2 Å(2), but similar to AL of DLPE=41 Å(2), consistent with untilted chains in gel phase TMCL.</div>
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