Magnetic resonance of lipids and proteins in membranes

Marsh, Derek

doi:10.1016/s1359-0294(97)80003-9

Cited by 12 publications

(3 citation statements)

References 86 publications

(44 reference statements)

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“…The phospholipid dimyristoyl phosphatidylcholine (DMPC) was obtained from Avanti Polar Lipids (Birmingham, AL, USA). Spin-labelled phosphatidylcholines ( n -PCSL) with the nitroxide group at different positions, n , in the sn -2 acyl chain were synthesized as described by Marsh and Watts (1982; Marsh 1997 ). The spin-labels were stored at −20°C in ethanol solutions at a concentration of 1 mg/ml.…”

Section: Methodsmentioning

confidence: 99%

Interaction of short modified peptides deriving from glycoprotein gp36 of feline immunodeficiency virus with phospholipid membranes

et al. 2009

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A tryptophan-rich octapeptide, C8 (Ac-TrpGlu-Asp-Trp-Val-Gly-Trp-Ile-NH 2 ), modelled on the membrane-proximal external region of the feline immunodeWciency virus (FIV) gp36 glycoprotein ectodomain, exhibits potent antiviral activity against FIV. A mechanism has been proposed by which the peptide, being positioned on the surface of the cell membrane, inhibits its fusion with the virus. In the present work, peptide-lipid interactions of C8 with dimyristoyl phosphatidylcholine liposomes are investigated using electron spin resonance spectroscopy of spin-labelled lipids. Three other peptides, obtained from modiWcations of C8, have also been investigated, in an attempt to clarify the essential molecular features of the interactions involving the tryptophan residues. The results show that C8 adsorbs strongly on the bilayer surface. Membrane binding requires not only the presence of the Trp residues in the sequence, but also their common orientation on one side of the peptide that is engendered by the WX 2 WX 2 W motif. Membrane interaction correlates closely with peptide antiviral activity, indicating that the membrane is essential in stabilizing the peptide conformation that will be able to inhibit viral infection.

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Section: Methodsmentioning

confidence: 99%

Interaction of short modified peptides deriving from glycoprotein gp36 of feline immunodeficiency virus with phospholipid membranes

et al. 2009

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“…ESR has been widely applied to investigations of membrane properties (Hubbell and McConnell, 1971;Berliner, 1976;Marsh, 1985;Freed, 1994Freed, , 2000, and has played an important role in identifying and characterizing the boundary lipid component in systems as diverse as cytochrome oxidase (Jost et al, 1973), rhodopsin (Watts et al, 1979), Na, K-transporting ATPase (Arora et al, 1999), and gramicidin A9 (GA) Freed, 1993, 1999;Marsh, 1997). The latter is a well-known system for studies of lipid-protein interactions due to the commercial availability of GA, its prompt incorporation into lipid bilayers, and its simple structure.…”

Section: Lipid-protein Interactions and Esrmentioning

confidence: 99%

Lipid-Gramicidin Interactions: Dynamic Structure of the Boundary Lipid by 2D-ELDOR

Costa-Filho¹,

Crepeau

Borbat

et al. 2003

Biophysical Journal

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The use of 2D-electron-electron double resonance (2D-ELDOR) for the characterization of the boundary lipid in membrane vesicles of DPPC and gramicidin A' (GA) is reported. We show that 2D-ELDOR, with its enhanced spectral resolution to dynamic structure as compared with continuous-wave electron spin resonance, provides a reliable and useful way of studying lipid-protein interactions. The 2D-ELDOR spectra of the end-chain spin label 16-PC in DPPC/GA vesicles is composed of two components, which are assigned to the bulk lipids (with sharp auto peaks and crosspeaks) and to the boundary lipids (with broad auto peaks). Their distinction is clearest for higher temperatures and higher GA concentrations. The quantitative analysis of these spectra shows relatively faster motions and very low ordering for the end chain of the bulk lipids, whereas the boundary lipids show very high "y-ordering" and slower motions. The y-ordering represents a dynamic bending at the end of the boundary lipid acyl chain, which can then coat the GA molecules. These results are consistent with the previous studies by Ge and Freed (1999) using continuous-wave electron spin resonance, thereby supporting their model for GA aggregation and H(II) phase formation for high GA concentrations. Improved instrumental and simulation methods have been employed.

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“…Cholesterol (CHOL) was obtained from Sigma. Spin‐labeled phosphatidylcholines ( n ‐PCSL) with the nitroxide group at different positions, n , in the sn ‐2 acyl chain were synthesized as described by Marsh and Watts37, 38. The spin‐labels were stored at − 20 °C in ethanol solutions at a concentration of 1 mg/ml.…”

Section: Methodsmentioning

confidence: 99%

Interaction of a β‐sheet breaker peptide with lipid membranes

Vitiello¹,

Grimaldi

Ramunno

et al. 2010

Journal of Peptide Science

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Aggregation of beta-amyloid peptides into senile plaques has been identified as one of the hallmarks of Alzheimer's disease. An attractive therapeutic strategy for Alzheimer's disease is the inhibition of the soluble beta-amyloid aggregation using synthetic beta-sheet breaker peptides that are capable of binding Abeta but are unable to become part of a beta-sheet structure. As the early stages of the Abeta aggregation process are supposed to occur close to the neuronal membrane, it is strategic to define the beta-sheet breaker peptide positioning with respect to lipid bilayers. In this work, we have focused on the interaction between the beta-sheet breaker peptide acetyl-LPFFD-amide, iAbeta5p, and lipid membranes, studied by ESR spectroscopy, using either peptides alternatively labeled at the C- and at the N-terminus or phospholipids spin-labeled in different positions of the acyl chain. Our results show that iAbeta5p interacts directly with membranes formed by the zwitterionic phospholipid dioleoyl phosphatidylcholine and this interaction is modulated by inclusion of cholesterol in the lipid bilayer formulation, in terms of both peptide partition coefficient and the solubilization site. In particular, cholesterol decreases the peptide partition coefficient between the membrane and the aqueous medium. Moreover, in the absence of cholesterol, iAbeta5p is located between the outer part of the hydrophobic core and the external hydrophilic layer of the membrane, while in the presence of cholesterol it penetrates more deeply into the lipid bilayer.

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Magnetic resonance of lipids and proteins in membranes

Cited by 12 publications

References 86 publications

Interaction of short modified peptides deriving from glycoprotein gp36 of feline immunodeficiency virus with phospholipid membranes

Interaction of short modified peptides deriving from glycoprotein gp36 of feline immunodeficiency virus with phospholipid membranes

Lipid-Gramicidin Interactions: Dynamic Structure of the Boundary Lipid by 2D-ELDOR

Interaction of a β‐sheet breaker peptide with lipid membranes

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