Selectivity of interaction of spin-labelled lipids with peripheral proteins bound to dimyristoylphosphatidylglycerol bilayers, as determined by ESR spectroscopy

Sankaram, M. B.; Kruijff, Ben de; Marsh, Derek

doi:10.1016/0005-2736(89)90483-5

Cited by 34 publications

(27 citation statements)

References 18 publications

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“…In addition, we observed a much smaller LD signal from cyt c upon CL incorporation, indicating poorer alignment within the membrane. The overall lower a-helicity of cyt c associated to CL vesicles suggests that the protein partially unfolds upon interaction with CL lipids, and is in agreement with previous observations that CL may induce loosening of the cyt c tertiary structure (52,58). No significant changes could however be observed in the Soret region of the CD spectrum.…”

Section: Discussionsupporting

confidence: 91%

Assigning Membrane Binding Geometry of Cytochrome c by Polarized Light Spectroscopy

Caesar

Esbjörner

Lincoln

et al. 2009

Biophysical Journal

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In this work we demonstrate how polarized light absorption spectroscopy (linear dichroism (LD)) analysis of the peptide ultraviolet-visible spectrum of a membrane-associated protein (cytochrome (cyt) c) allows orientation and structure to be assessed with quite high accuracy in a native membrane environment that can be systematically varied with respect to lipid composition. Cyt c binds strongly to negatively charged lipid bilayers with a distinct orientation in which its alpha-helical segments are on average parallel to the membrane surface. Further information is provided by the LD of the pi-pi( *) transitions of the heme porphyrin and transitions of aromatic residues, mainly a single tryptophan. A good correlation with NMR data was found, and combining NMR structural data with LD angular data allowed the whole protein to be docked to the lipid membrane. When the redox state of cyt c was changed, distinct variations in the LD spectrum of the heme Soret band were seen corresponding to changes in electronic transition energies; however, no significant change in the overall protein orientation or structure was observed. Cyt c is known to interact in a specific manner with the doubly negatively charged lipid cardiolipin, and incorporation of this lipid into the membrane at physiologically relevant levels was indeed found to affect the protein orientation and its alpha-helical content. The detail in which cyt c binding is described in this study shows the potential of LD spectroscopy using shear-deformed lipid vesicles as a new methodology for exploring membrane protein structure and orientation.

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Section: Discussionsupporting

confidence: 91%

Assigning Membrane Binding Geometry of Cytochrome c by Polarized Light Spectroscopy

Caesar

Esbjörner

Lincoln

et al. 2009

Biophysical Journal

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“…Besides the relevance of membrane surface charge and lipid chain ordering, our results also indicate a significant selectivity of different lipids for interaction with the peptides. Under certain assumptions, including those of fast lipid exchange on the spin-label EPR time scale, the increase in outer hyperfine splitting, ΔA max , for different 5-position spin-labeled lipid species can be related to their relative association constants with the protein [45,46]. The lipid selectivity pattern for interaction with the gH626-644 peptide in DMPC is in the order: PA ≈ PG ≈ PS N PE ≈ PC, and that for the gB632-6509 peptide is PS N PG ≈ PA N PE ≈ PC (see Table 1).…”

Section: Discussionmentioning

confidence: 99%

“…The selectivity of interaction of different lipids with the gH626-644 or gB632-650 peptide bound to DMPC membranes was determined by using probe amounts of lipids spin labeled at the 5-C atom of the sn-2 chain [45,46]. Table 1 gives the values of the outer hyperfine splitting, 2A max , for the spin labels at 30°C, in the presence and absence of 1:1 wt/ wt peptide.…”

Section: Selectivity Of Lipid-peptide Interactionmentioning

confidence: 99%

Lipid composition modulates the interaction of peptides deriving from herpes simplex virus type I glycoproteins B and H with biomembranes

Vitiello

Falanga

Galdiero

et al. 2011

Biochimica et Biophysica Acta (BBA) - Biomembranes

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Lipid membranes play a key role in the viral life cycle. Enveloped viruses particularly require a sequence of fusion and fission events between the viral envelope and the target membranes for entry into the cell and egress from it. These processes are controlled by one or more viral glycoproteins that undergo conformational changes favoring the necessary micro- and mesoscopic lipid re-arrangements. Multiple regions from these glycoproteins are thought to interact with the membranes, according to a concerted mechanism, in order to generate the distortion necessary for fusion. In this work, we perform an EPR study on the role played by the membrane composition in tuning the interaction between lipid bilayers and two peptides, gH626-644 and gB632-650, that are highly fusogenic fragments of the gH and gB glycoproteins of herpes simplex virus. Our results show that both peptides interact with lipid bilayers, perturbing the local lipid packing. gH626-644 localizes close to the hydrophilic bilayer surface, while gB632-650 penetrates deeply into the membrane. Chain perturbation by the peptides increases in the presence of charged phospholipids. Finally, cholesterol does not alter the ability of gB632-650 to penetrate deeply in the membrane, whereas it limits penetration of the gH626-644 peptide to the more external layer. The different modes of interaction result in a higher fusogenic ability of gB632-650 towards cholesterol-enriched membranes, as demonstrated by lipid mixing assays. These results suggest that the mechanism of action of the gH and gB glycoproteins is modulated by the properties and composition of the phospholipid bilayer.

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“…The perturbation of the mobility of spin-labeled lipids with different polar headgroups by binding tetralysine, pentalysine, and polylysine was determined for lipid probes spin labeled at the 5 C-atom position of the chain to establish the selectivity of interaction of the different lipid species with these basic peptides (cf. Sankaram et al, 1989b). Measurements were made at 30°C on DMPG host bilayers for all three peptides and additionally on DMPS lipid matrices at 44'C for pentalysine, with a concentration of 1 mol% of the various spin-labeled lipid species.…”

Section: Interaction With Different Spin-labeled Lipid Speciesmentioning

confidence: 99%

Spin-label electron spin resonance studies on the interactions of lysine peptides with phospholipid membranes

Kleinschmidt¹,

Marsh²

1997

Biophysical Journal

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The interactions of lysine oligopeptides with dimyristoyl phosphatidylglycerol (DMPG) bilayer membranes were studied using spin-labeled lipids and electron spin resonance spectroscopy. Tetralysine and pentalysine were chosen as models for the basic amino acid clusters found in a variety of cytoplasmic membrane-associating proteins, and polylysine was chosen as representative of highly basic peripherally bound proteins. A greater motional restriction of the lipid chains was found with increasing length of the peptide, while the saturation ratio of lipids per peptide was lower for the shorter peptides. In DMPG and dimyristoylphosphatidylserine host membranes, the perturbation of the lipid chain mobility by polylysine was greater for negatively charged spin-labeled lipids than for zwitterionic lipids, but for the shorter lysine peptides these differences were smaller. In mixed bilayers composed of DMPG and dimyristoylphosphatidylcholine, little difference was found in selectivity between spin-labeled phospholipid species on binding pentalysine. Surface binding of the basic lysine peptides strongly reduced the interfacial pK of spin-labeled fatty acid incorporated into the DMPG bilayers, to a greater extent for polylysine than for tetralysine or pentalysine at saturation. The results are consistent with a predominantly electrostatic interaction with the shorter lysine peptides, but with a closer surface association with the longer polylysine peptide.

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Selectivity of interaction of spin-labelled lipids with peripheral proteins bound to dimyristoylphosphatidylglycerol bilayers, as determined by ESR spectroscopy

Cited by 34 publications

References 18 publications

Assigning Membrane Binding Geometry of Cytochrome c by Polarized Light Spectroscopy

Assigning Membrane Binding Geometry of Cytochrome c by Polarized Light Spectroscopy

Lipid composition modulates the interaction of peptides deriving from herpes simplex virus type I glycoproteins B and H with biomembranes

Spin-label electron spin resonance studies on the interactions of lysine peptides with phospholipid membranes

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