Molecular Organization in Striated Domains Induced by Transmembrane α-Helical Peptides in Dipalmitoyl Phosphatidylcholine Bilayers

Sparr, Emma; Ganchev, Dragomir N.; Snel, M. M. E.; Ridder, Anja N. J. A.; Kroon-Batenburg, Loes M. J.; Chupin, Vladimir; Rijkers, Dirk T. S.; Killian, J. Antoinette; Kruijff, Ben de

doi:10.1021/bi048047a

Cited by 19 publications

(53 citation statements)

References 31 publications

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“…In principle, it is possible that these results are simply because of more favorable excimer formation by pyrene moieties in antiparallel peptides than in parallel peptides. However, this is unlikely, because we have previously shown that excimer formation also occurs in parallel peptides under certain conditions (18). Therefore, the most straightforward interpretation of our data is that there is only direct contact between antiparallel helices.…”

Section: Helix-helix Association As Analyzed By Pyrene Excimer Fluorementioning

confidence: 66%

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Self-association of Transmembrane α-Helices in Model Membranes

Sparr

Ash

Nazarov

et al. 2005

Journal of Biological Chemistry

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127

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Interactions between transmembrane helices play a key role in almost all cellular processes involving membrane proteins. We have investigated helix-helix interactions in lipid bilayers with synthetic tryptophan-flanked peptides that mimic the membrane spanning parts of membrane proteins. The peptides were functionalized with pyrene to allow the self-association of the helices to be monitored by pyrene fluorescence and Trp-pyrene fluorescence resonance energy transfer (FRET). Specific labeling of peptides at either their N or C terminus has shown that helix-helix association occurs almost exclusively between antiparallel helices. Furthermore, computer modeling suggested that antiparallel association arises primarily from the electrostatic interactions between ␣-helix backbone atoms. We propose that such interactions may provide a force for the preferentially antiparallel association of helices in polytopic membrane proteins. Helix-helix association was also found to depend on the lipid environment. In bilayers of dioleoylphosphatidylcholine, in which the hydrophobic length of the peptides approximately matched the bilayer thickness, association between the helices was found to require peptide/lipid ratios exceeding 1/25. Selfassociation of the helices was promoted by either increasing or decreasing the bilayer thickness, and by adding cholesterol. These results indicate that helix-helix association in membrane proteins can be promoted by unfavorable protein-lipid interactions.Most membrane proteins have one or more hydrophobic segments that span the membrane in an ␣-helical conformation. Interactions between these transmembrane (TM) 4 helices are important for determining the structure of multispanning membrane proteins and for assembly of membrane proteins into oligomeric structures (1-4). Several factors are thought to be responsible for the association of helices in membrane proteins, including surface complementarity, the presence of polar residues in the transmembrane region (5-7), and certain specific motifs such as the well known GXXXG pattern (8, 9). It is likely that several of these factors act in concert to determine the final folded structure, or the association of monomers to form an oligomer. In addition to helix-helix interactions, interactions between the helices and surrounding lipids also play a role in the organization and assembly of TM helices. For example, even when helices do not exhibit any tendency to undergo specific association (10 -12), helix-helix association could still occur as a result of poor packing between the lipids and helices, or from a favorable change in entropy resulting from the release of helix-bound lipids upon helix association. In these cases, helix association is primarily driven by lipid-protein interactions rather than strongly favorable protein-protein interactions. It is likely that in real membrane proteins the driving forces for folding involve both types of interaction, whether or not specific protein-protein recognition motifs are present.One property of a pr...

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Section: Helix-helix Association As Analyzed By Pyrene Excimer Fluorementioning

confidence: 66%

“…The pyrenelabeled peptides pyr N -WALP23 (Ac-C(pyrene)-GWW(LA) 8 LWWAamide) and pyr C -WALP23 (Ac-GWW(LA) 8 LWWGC(pyrene)-amide) were synthesized as described earlier (18). The fluorescent probe N-(1-pyrene)maleimide was obtained from Molecular Probes Europe BV (Leiden, The Netherlands).…”

Section: Methodsmentioning

confidence: 99%

Self-association of Transmembrane α-Helices in Model Membranes

Sparr

Ash

Nazarov

et al. 2005

Journal of Biological Chemistry

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127

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“…The model depicts the striated domains as a regular array of linetype depressions with a repeat distance of 8 nm and consisting of linear peptide aggregates flanked by some lipids that are disordered and have lost their acyl chain tilt. Subsequent research using multiple techniques showed that these initial models were largely correct (Sparr et al, 2005). Gold-labeling experiments showed that the peptides were localized in the line-type depressions and in the striated domains.…”

Section: Molecular Organization Of Striated Domainsmentioning

confidence: 99%

“…The domain thus is the end result of peptide-peptide interactions in the linear peptide aggregate and lipid-peptide interactions along the peptide arrays. These insights into the organization of the line-type depressions and the striated domains, together with studies on the temperature dependence of these systems, led to a proposal of the mechanism of formation of the striated domains (Sparr et al, 2005). …”

Section: Molecular Organization Of Striated Domainsmentioning

confidence: 99%

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

Kruijff¹,

Killian²,

Ganchev³

et al. 2006

Biological Chemistry

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This review summarizes the knowledge on striated domains, which are ordered assemblies of transmembrane peptides and lipids under gel-state conditions. The structure, mechanism of function and utility of this system as a model for domain formation is described, resulting in a molecular description of the domains and a discussion on the relevance of these insights for the function/formation and structure of similar domains in biological membranes.

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“…Of special interest is the lateral heterogeneity induced by WALP in otherwise smooth DPPC bilayers as mixed lipid/peptide microdomains with a distinct striated appearance are spontaneously formed (Rinia et al, 2002). The striated pattern is built-up from rows of gel-state lipids with a modified packing, which alternate with single rows of the shorter WALP23 (Sparr et al, 2005). Driving forces are believed to be competing lipid packing effects and lipid-peptide interactions.…”

Section: Introductionmentioning

confidence: 99%

AFM study of the thermotropic behaviour of supported DPPC bilayers with and without the model peptide WALP23

Yarrow

Kuipers

2011

Chemistry and Physics of Lipids

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Temperature-controlled Atomic Force Microscopy (TC-AFM) in Contact Mode is used here to directly image the mechanisms by which melting and crystallization of supported, hydrated DPPC bilayers proceed in the presence and absence of the model peptide WALP23. Melting from the gel L(β)' to the liquid-crystalline L(α) phase starts at pre-existing line-type packing defects (grain boundaries) in absence of the peptide. The exact transition temperature is shown to be influenced by the magnitude of the force exerted by the AFM probe on the bilayer, but is higher than the main transition temperature of non-supported DPPC vesicles in all cases due to bilayer-substrate interactions. Cooling of the fluid L(α) bilayer shows the formation of the line-type defects at the borders between different gel-phase regions that originate from different nuclei. The number of these defects depends directly on the rate of cooling through the transition, as predicted by classical nucleation theory. The presence of the transmembrane, synthetic model peptide WALP23 is known to give rise to heterogeneity in the bilayer as microdomains with a striped appearance are formed in the DPPC bilayer. This striated phase consists of alternating lines of lipids and peptide. It is shown here that melting starts with the peptide-associated lipids in the domains, whose melting temperature is lowered by 0.8-2.0°C compared to the remaining, peptide-free parts of the bilayer. The stabilization of the fluid phase is ascribed to adaptations of the lipids to the shorter peptide. The lipids not associated with the peptide melt at the same temperature as those in the pure DPPC supported bilayer.

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Molecular Organization in Striated Domains Induced by Transmembrane α-Helical Peptides in Dipalmitoyl Phosphatidylcholine Bilayers

Cited by 19 publications

References 31 publications

Self-association of Transmembrane α-Helices in Model Membranes

Self-association of Transmembrane α-Helices in Model Membranes

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

AFM study of the thermotropic behaviour of supported DPPC bilayers with and without the model peptide WALP23

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