Striated domains: self-organizing ordered assemblies of transmembrane α-helical peptides and lipids in bilayers

Kruijff, Ben de; Killian, J. Antoinette; Ganchev, Dragomir N.; Rinia, Hilde A.; Sparr, Emma

doi:10.1515/bc.2006.031

Cited by 11 publications

(15 citation statements)

References 16 publications

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“…It is not clear whether they correspond to external or internal structures and further experiments are needed to clarify their nature. In other microorganisms, striped domains have been observed in gas vesicle membranes [22], [23], in the peptidoglycan cell wall of some bacteria [24] and as protein-lipid domains in cellular membranes [25].…”

Section: Discussionmentioning

confidence: 99%

Morphological and Structural Aspects of the Extremely Halophilic Archaeon Haloquadratum walsbyi

et al. 2011

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Ultrathin square cell Haloquadratum walsbyi from the Archaea domain are the most abundant microorganisms in the hypersaline water of coastal salterns and continental salt lakes. In this work, we explore the cell surface of these microorganisms using amplitude-modulation atomic-force microscopy in nearly physiological conditions. We demonstrate the presence of a regular corrugation with a periodicity of 16–20 nm attributed to the surface layer (S-layer) protein lattice, striped domains asymmetrically distributed on the cell faces and peculiar bulges correlated with the presence of intracellular granules. Besides, subsequent images of cell evolution during the drying process indicate the presence of an external capsule that might correspond to the giant protein halomucin, predicted by the genome but never before observed by other microscopy studies.

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Section: Discussionmentioning

confidence: 99%

Morphological and Structural Aspects of the Extremely Halophilic Archaeon Haloquadratum walsbyi

et al. 2011

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“…It belongs to a family of proteins possessing a core of alternating hydrophobic leucine and alanine residues, with hydrophilic tryptophan ends. Using atomic force microscopy (AFM), de Kruijff observed the surface organization and hexagonal packing of WALP23 peptides in the gel phase of a dipalmitoylphosphatidylcholine (DPPC) lipid bilayer [6]. Atomic force microscopy shows that the presence of the peptides in a supported bilayer of DPPC affects the morphology of the membrane.…”

Section: Introductionmentioning

confidence: 99%

Coarse-grained simulation of transmembrane peptides in the gel phase

Al-Lehyani

Grime

Bano

et al. 2013

Journal of Computational Physics

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We use Dissipative Particle Dynamics simulations, combined with parallel tempering and umbrella sampling, to investigate the potential of mean force between model transmembrane peptides in the various phases of a lipid bilayer, including the low-temperature gel phase. The observed oscillations in the effective interaction between peptides are consistent with the different structures of the surrounding lipid phases.

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“…The peptide was modelled to mimic one of the α-helical, transmembrane units that are often found in membrane-spanning proteins and can therefore provide insight into the factors regulating the organization of protein subunits in the membrane. Interestingly, insertion of WALP into gel-phase bilayers of saturated PC lipids leads to self-assembled, regular patterns of alternating rows of WALP and rows of lipids with a modified conformation (De Kruijff et al 2006; Sparr et al 2005). The driving forces for the formation of this so-called striated phase are believed to involve direct lipid-peptide interactions and packing requirements of the lipids in the bilayer.…”

Section: Introductionmentioning

confidence: 99%

“…It may equally be expected that other changes in the lipid matrix, as introduced through the presence of the cis bond, will also lead to changes in the formation of the lateral distribution of the WALP23. However, up till now, saturated PC lipids have exclusively been used in the AFM studies (Rinia et al 2000; De Kruijff et al 2006). The results of this study could serve to enhance our understanding of the exact contribution of all involved driving forces determining lateral distribution of proteins.…”

Section: Introductionmentioning

confidence: 99%

An AFM study of solid-phase bilayers of unsaturated PC lipids and the lateral distribution of the transmembrane model peptide WALP23 in these bilayers

Yarrow

2011

Eur Biophys J

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An altered lipid packing can have a large influence on the properties of the membrane and the lateral distribution of proteins and/or peptides that are associated with the bilayer. Here, it is shown by contact-mode atomic force microscopy that the surface topography of solid-phase bilayers of PC lipids with an unsaturated cis bond in their acyl chains shows surfaces with a large number of line-type packing defects, in contrast to the much smoother surfaces observed for saturated PC lipids. Di-n:1-PC (n = 20, 22, 24) and (16:0,18:1)-PC (POPC) were used. Next, the influence of an altered lipid environment on the lateral distribution of the single α-helical model peptide WALP23 was studied by incorporating the peptide in the bilayers of di-n:1-PC (n = 20, 22, 24) and (16:0,18:1)-PC unsaturated lipids. The presence of WALP23 leads to an increase in the number of packing defects but does not lead to the formation of the striated domains that were previously observed in bilayers of saturated PC lipids and WALP. This is ascribed to the less efficient lateral lipid packing of the unsaturated lipids, while the increase in packing defects is probably an indirect effect of the peptide. Finally, the fact that an altered lipid packing affects the distribution of WALP23 is also confirmed in an additional experiment where the solvent TFE (2,2,2-trifluorethanol) is added to bilayers of di-16:0-PC/WALP23. At 3.5 vol% TFE, the previous striated ordering of the peptide is abolished and replaced by loose lines.

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Striated domains: self-organizing ordered assemblies of transmembrane α-helical peptides and lipids in bilayers

Cited by 11 publications

References 16 publications

Morphological and Structural Aspects of the Extremely Halophilic Archaeon Haloquadratum walsbyi

Morphological and Structural Aspects of the Extremely Halophilic Archaeon Haloquadratum walsbyi

Coarse-grained simulation of transmembrane peptides in the gel phase

An AFM study of solid-phase bilayers of unsaturated PC lipids and the lateral distribution of the transmembrane model peptide WALP23 in these bilayers

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