Chapter 2 Membrane Lipid Molecular Structure and Polymorphism

Lewis, Richard L.; Mannock, David A.; McElhaney, Ronald N.

doi:10.1016/s0070-2161(08)60206-3

Cited by 46 publications

(36 citation statements)

References 118 publications

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“…The structural data here presented indicated that the main effect of the C2-substitution is the modulation of the FA density distributions rather than the extent of the H-bond network within the interfacial region of the membrane. Considering the macroscopic "molecular shape model" ( 9 ) and assuming a similar molecular geometry for all DEPE:FA systems studied, the primary reason for the 2OHOA, OA, and 2MOA differential effect on the thermotropic behavior of DEPE membranes could be related to the FA effect on the headgroup area at the lipid-water interface, because the acyl chain packing would be similar for all systems. The shift of 2OHOA toward the outer side of the membrane will be associated with a higher optimum headgroup area that could account for the appearance of the L ␣ -to-H II phase transition at higher temperatures and the stabilization of the L ␣ phase, as observed experimentally.…”

Section: Discussionmentioning

confidence: 99%

“…In fact, PE lipids have an intrinsic propensity to segregate forming nonlamellar H II structures in vitro ( 9 ), and some special features were attributed to H II -prone phospholipids, such as the functional control of membrane proteins and the structural organization inside cells (10)(11)(12). On the other hand, FAs incorporated in phospholipids or present in the membrane in their unesterifi ed form are able to modulate the structure of model PE membranes by interacting specifi cally with the latter ( 13,14 ).…”

Section: Molecular Dynamics Simulationsmentioning

confidence: 99%

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Interactions of fatty acids with phosphatidylethanolamine membranes: X-ray diffraction and molecular dynamics studies

Cordomí

Prades

Frau

et al. 2010

Journal of Lipid Research

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An experimental and theoretical study on 1,2-dielaidoyl -sn -glycero -3-phosphoethanolamine (DEPE) membranes containing fatty acids (FAs) was performed by means of X-ray diffraction analysis and molecular dynamics (MD) simulations. The study was aimed at understanding the interactions of several structurally related FAs with biomembranes, which is necessary for further rational lipid drug design in membrane-lipid therapy.

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Section: Discussionmentioning

confidence: 99%

Section: Molecular Dynamics Simulationsmentioning

confidence: 99%

Interactions of fatty acids with phosphatidylethanolamine membranes: X-ray diffraction and molecular dynamics studies

Cordomí

Prades

Frau

et al. 2010

Journal of Lipid Research

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“…(1 for DEPE and DPPC membranes that were attributed to hydrated and dehydrated carbonyl groups of phospholipids, respectively [39]. DPPC samples did not change at all in the presence of any of the peptides used in these studies.…”

Section: Peptide-lipid Interactions Determined By Ftirmentioning

confidence: 72%

“…Again none of the peptides produced any significant changes in the DPPC membranes and therefore, we did not pursue their study any further. However, in DEPE membranes, the frequency of the methylene stretching band was decreased by all peptides in a concentration dependent manner, which has been associated with an increase in the hydrocarbon chain conformational order in the bilayer core [39]. Nonetheless, the L b -to-L a phase transition temperature as monitored by such frequency was not altered by presence of any of the peptides.…”

Section: Peptide-lipid Interactions Determined By Ftirmentioning

confidence: 79%

Interaction of transmembrane-spanning segments of the α2-adrenergic receptor with model membranes

Prades

Encinar

Funari³

et al. 2009

Molecular Membrane Biology

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Full terms and conditions of use: http://www.informaworld.com/terms-and-conditions-of-access.pdf This article may be used for research, teaching and private study purposes. Any substantial or systematic reproduction, re-distribution, re-selling, loan or sub-licensing, systematic supply or distribution in any form to anyone is expressly forbidden.The publisher does not give any warranty express or implied or make any representation that the contents will be complete or accurate or up to date. The accuracy of any instructions, formulae and drug doses should be independently verified with primary sources. The publisher shall not be liable for any loss, actions, claims, proceedings, demand or costs or damages whatsoever or howsoever caused arising directly or indirectly in connection with or arising out of the use of this material.Interaction of transmembrane-spanning segments of the a2-adrenergic receptor with model membranes AbstractAdrenergic receptors are integral membrane proteins involved in cellular signalling that belong to the G protein-coupled receptors. Synthetic peptides resembling the putative transmembrane (TM) segments TM4, TM6 and TM7, of the human a2-adrenergic receptor subtype C10 (P08913) and defined lipid vesicles were used to assess protein-lipid interactions that might be relevant to receptor structure/function. P6 peptide contains the hydrophobic core of TM6 plus the N-terminal hydrophilic motif REKR, while peptides P4 and P7 contained just the hydrophobic stretches of TM4 and TM7, respectively. All the peptides increase their helical tendency at moderate concentrations of TFE (30Á50%) and in presence of 1,2-dielaidoyl-sn-glycero-3-phosphatidylethanolamine (DEPE) lipids. However, only P6 displays up to 19% of a-helix in the presence of just the DEPE lipids, evidences a transmembrane orientation and stabilizes the La lipid phase. Conversely, P4 and P7 peptides form only stable b-sheet structures in DEPE and favour the non-lamellar, inverted hexagonal (H II ) phase of DEPE by lowering its phase transition temperature. This study highlights the potential of using synthetic peptides derived from the amino acid sequence in the native proteins as templates to understand the behaviour of the transmembrane segments and underline the importance of interfacial anchoring interactions to meet hydrophobic matching requirements and define membrane organization.

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“…The characterization of real biological systems is considered a diffi cult task due to their complexity. Therefore, the physicochemical properties of model, biologically relevant, binary or ternary lamellar and nonlamellar phases Hyde et al, 1997 ;Lewis et al, 1998 ;Lindblom and Rilfors, 1989 ;Ortiz et al, 1999 ;Yaghmur et al, 2007 ) as well as their corresponding nanostructured dispersions have received considerable attention (Angelova et al, 2005 ;Barauskas et al, 2005 ;Gustafsson et al, 1996 ;Larsson, 2000 ;Rizwan et al, 2007 ;Spicer, 2004 ). In this context, numerous investigations have been carried out on the physicochemical properties and the phase behavior of biologically relevant surfactant -like lipid -water systems (Barauskas and Landh, 2003 ;de Campo et al, 2004 ;Larsson, 1983 ;Lindblom et al, 1979 ;Lutton, 1965 ;Caffrey, 1998, 1999 ), particularly the temperature -water content phase diagrams of various binary monoglyceride -water systems (Larsson, 1983 ;Lindblom et al, 1979 ;Lutton, 1965 ).…”

Section: Introductionmentioning

confidence: 99%