Parameters modulating the maximum insertion pressure of proteins and peptides in lipid monolayers

Calvez, Philippe; Bussières, Sylvain; Demers, Éric; Salesse, Christian

doi:10.1016/j.biochi.2009.03.018

Cited by 143 publications

(224 citation statements)

References 132 publications

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“…The 95% confidence intervals for these values are calculated according to (49). We note that the insertion of the -helix bundle of perilipin 3 is highest for POG and POPE, both of which have negative spontaneous curvature, took a considerable time for perilipin 3D to start inserting into the DOPC monolayer (see supplemental Fig.…”

Section: Addition Of Further Domains Of the N Terminus Results In A Rmentioning

confidence: 99%

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Insertion of perilipin 3 into a glycero(phospho)lipid monolayer depends on lipid headgroup and acyl chain species

Mirheydari

Rathnayake

Frederick

et al. 2016

Journal of Lipid Research

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function of LDs. While much work has focused on peripheral and integral membrane proteins, the mechanism by which LD binding proteins recognize and target to LDs is still poorly understood (1). This is especially true for dedicated LD binding proteins of the perilipin family, i.e., perilipin 1 through 5, that function in the biogenesis and metabolism (lipolysis) of LDs. No work has directly investigated the interaction of a perilipin family member with a phospholipid monolayer interface. In order to address how this family of proteins interacts with lipid interfaces, we investigated the interaction of perilipin 3 with phospholipid monolayers at the air-buffer interface. We chose perilipin 3 because it is found in the cytosol as well as on the LD surface, and because previous work has characterized the structure and LD association of the protein (1-3).In addition to providing cellular energy, LDs take part in many other cellular functions, including signal transduction, formation of new cellular membranes, hormone synthesis, and lipid trafficking (4-8). Under certain physiological conditions, LDs have been found to act as storehouses for several different types of enzymes and proteins, including histones (9, 10), and they also facilitate virus replication (11-13). An understanding of how proteins Lipid droplets (LDs) are dynamic cell organelles that carry out a multitude of cellular functions vital for life, and protein-lipid interactions are crucial to the structure and

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Section: Addition Of Further Domains Of the N Terminus Results In A Rmentioning

confidence: 99%

“…The Langmuir monolayer technique is a biophysical method frequently used to explore the lipid interaction of proteins and peptides, specifically protein insertion (49,50).…”

mentioning

confidence: 99%

Insertion of perilipin 3 into a glycero(phospho)lipid monolayer depends on lipid headgroup and acyl chain species

Mirheydari

Rathnayake

Frederick

et al. 2016

Journal of Lipid Research

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“…Phospholipid monolayers are very useful model membranes to study lipid-protein or lipidpeptide interactions (for a review, see [114][115][116][117][118][119][120][121][122][123][124][125]). Indeed, it allows to control several physical parameters such as the density of lipids and the surface pressure, the subphase content, the lipid composition, etc.…”

Section: Monolayers As a Model Membrane To Study Hydrophobic Transmemmentioning

confidence: 99%

“…Unfortunately, these two approaches have never been systematically compared although they could potentially provide complementary information. The observation of an increase in surface pressure is restricted by the maximum insertion pressure (MIP) of the peptide (see section 4.5; for a review, see [116]). The MIP corresponds to the maximum surface pressure of the monolayer up to which the peptide can insert in the monolayer and beyond which no insertion takes place.…”

Section: Preparation Of Lipid Monolayers To Study Hydrophobic Transmementioning

confidence: 99%

“…Indeed, given that the membrane lateral pressure has been estimated in the range of 30-35 mN/m [206][207][208][209][210][211][212][213], one can postulate that a MIP larger than this value will suggest that the peptide could bind membranes. The synergy is obtained by adding 1 to the slope of the plot of the surface pressure increase (ΔΠ) as a function of the initial surface pressure (Π i ) [116]. We have previously shown that a positive synergy corresponds to a favorable binding of proteins.…”

Section: Preparation Of Lipid Monolayers To Study Hydrophobic Transmementioning

confidence: 99%

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Comparison between the behavior of different hydrophobic peptides allowing membrane anchoring of proteins

Lhor¹,

Bernier²,

Horchani³

et al. 2014

Advances in Colloid and Interface Science

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Membrane binding of proteins such as short chain dehydrogenases reductases or tail-anchored proteins relies on their N-and/or C-terminal hydrophobic transmembrane segment. In this review, we propose guidelines to characterize such hydrophobic peptide segments using spectroscopic and biophysical measurements. The secondary structure content of the C-terminal peptides of retinol dehydrogenase 8, RGS9-1 anchor protein, lecithin retinol acyl transferase, and of the N-terminal peptide of retinol dehydrogenase 11 has been deduced by prediction tools from their primary sequence as well as by using infrared or circular dichroism analyses. Depending on the solvent and the solubilization method, significant structural differences were observed, often involving α-helices. The helical structure of these peptides was found to be consistent with their presumed membrane binding. Langmuir monolayers have been used as membrane models to study lipidpeptide interactions. The values of maximum insertion pressure obtained for all peptides using a monolayer of 1,2-dioleoyl-sn-glycero-3-phospho-ethanolamine (DOPE) are larger than the estimated lateral pressure of membranes, thus suggesting that they bind membranes. Polarization modulation infrared reflection absorption spectroscopy has been used to determine the structure and orientation of these peptides in the absence and in the presence of a DOPE monolayer. This lipid induced an increase or a decrease in the organization of the peptide secondary structure. Further measurements are necessary using other lipids to better understand the membrane interactions of these peptides.

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Interaction of a Tat Substrate and a Tat Signal Peptide with Thylakoid Lipids at the Air–Water Interface

et al. 2011

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The Tat machinery enables folded proteins to be translocated across biological membranes. In vitro studies have shown that Tat substrates can interact with membranes prior to translocation. In this study we investigated the initial states of this interaction with thylakoid lipid monolayers at the air-water interface by using monolayer techniques combined with infrared reflection-absorption spectroscopy (IRRAS). We used enhanced green fluorescent protein (EGFP) as a model substrate and the signal peptide SP16 from the 16 kDa protein of the spinach oxygen-evolving complex (OEC16). We found that the signal peptide is essential for the interaction of the model substrate with lipid monolayers. IRRA spectroscopy showed an increased amount of α-helical secondary structure elements for the chimeric model substrate i16/EGFP (SP16 fused to EGFP) compared with EGFP; this can be attributed to the signal peptide.

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Parameters modulating the maximum insertion pressure of proteins and peptides in lipid monolayers

Cited by 143 publications

References 132 publications

Insertion of perilipin 3 into a glycero(phospho)lipid monolayer depends on lipid headgroup and acyl chain species

Insertion of perilipin 3 into a glycero(phospho)lipid monolayer depends on lipid headgroup and acyl chain species

Comparison between the behavior of different hydrophobic peptides allowing membrane anchoring of proteins

Interaction of a Tat Substrate and a Tat Signal Peptide with Thylakoid Lipids at the Air–Water Interface

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