Shape variation of bilayer membrane daughter vesicles induced by anisotropic membrane inclusions

Bohinc, Klemen; Lombardo, Darko; Kralj‐Iglič, Veronika; Fošnarič, Miha; May, Sylvio; Pernuš, Franjo; Hägerstrand, Henry; Iglič, Aleš

doi:10.2478/s11658-006-0009-3

Cited by 9 publications

(8 citation statements)

References 21 publications

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“…Although this is reasonable at low surface concentration, where our previous data indicate that the peptide is monomeric (9), we have no data to show this at high concentration. And pHLIP interaction with the outer leaflet of a bilayer creates strain and distortion, because anisotropic area occupancy induces bilayer distortions (18,19). We previously reported such a distortion induced by pHLIP interaction with the outer leaflet of the red blood cell membrane (8) as well as distortion in a liposome system (12).…”

Section: Discussionmentioning

confidence: 98%

Energetics Of Peptide (pHLIP) Binding To And Folding Across A Lipid Bilayer Membrane

Reshetnyak

Andreev

Segala

et al. 2009

Biophysical Journal

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Section: Discussionmentioning

confidence: 98%

Energetics Of Peptide (pHLIP) Binding To And Folding Across A Lipid Bilayer Membrane

Reshetnyak

Andreev

Segala

et al. 2009

Biophysical Journal

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“…116,117 The membrane-tubulating ability of these proteins suggests significant anisotropy in their method of curvature induction, and both energy-minimization and Monte Carlo simulation approaches have shown that these proteins should tend to cluster at the neck region of a budding vesicle. 116,117 This mechanism seems justifiable to rationalize the propensity for the association of the BAR domain, dynamin, or epsin in regions of negative Gaussian curvature. 68 Studies of anisotropic inclusions have shown that for certain choices of parameters even anisotropic curvature-inducing proteins can produce spherical buds.…”

Section: Mechanism and Biophysical Model For Membrane Deformation mentioning

confidence: 99%

“…68 Studies of anisotropic inclusions have shown that for certain choices of parameters even anisotropic curvature-inducing proteins can produce spherical buds. 116 These models suggest that the uniform spatial distribution of epsins on the clathrin coat (owing to the CLAP domain-mediated interaction) can be responsible for early invagination. However, as the coat matures into a bud, the emergence of a well defined-neck region with negative Gaussian curvature causes the epsins to migrate to the rim along with Eps15, suggesting a rich and dynamic set of events surrounding a nucleating CCP.…”

Section: Mechanism and Biophysical Model For Membrane Deformation mentioning

confidence: 99%

Systems biology and physical biology of clathrin-mediated endocytosis

et al. 2011

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In this review, we describe the application of experimental data and modeling of intracellular endocytic trafficking mechanisms with a focus on the process of clathrin-mediated endocytosis. A detailed parts-list for the protein–protein interactions in clathrin-mediated endocytosis has been available for some time. However, recent experimental, theoretical, and computational tools have proved to be critical in establishing a sequence of events, cooperative dynamics, and energetics of the intracellular process. On the experimental front, total internal reflection fluorescence microscopy, photo-activated localization microscopy, and spinning-disk confocal microscopy have focused on assembly and patterning of endocytic proteins at the membrane, while on the theory front, minimal theoretical models for clathrin nucleation, biophysical models for membrane curvature and bending elasticity, as well as methods from computational structural and systems biology, have proved insightful in describing membrane topologies, curvature mechanisms, and energetics.

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Section: (For 37°c) (B)mentioning

confidence: 99%

Energetics of peptide (pHLIP) binding to and folding across a lipid bilayer membrane

Reshetnyak

Andreev

Segala

et al. 2008

Proc. Natl. Acad. Sci. U.S.A.

166

180

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The pH low-insertion peptide (pHLIP) serves as a model system for peptide insertion and folding across a lipid bilayer. It has three general states: (I) soluble in water or (II) bound to the surface of a lipid bilayer as an unstructured monomer, and (III) inserted across the bilayer as a monomeric ␣-helix. We used fluorescence spectroscopy and isothermal titration calorimetry to study the interactions of pHLIP with a palmitoyloleoylphosphatidylcholine (POPC) lipid bilayer and to calculate the transition energies between states. We found that the Gibbs free energy of binding to a POPC surface at low pHLIP concentration (state I-state II transition) at 37°C is approximately ؊7 kcal/mol near neutral pH and that the free energy of insertion and folding across a lipid bilayer at low pH (state II-state III transition) is nearly ؊2 kcal/mol. We discuss a number of related thermodynamic parameters from our measurements. Besides its fundamental interest as a model system for the study of membrane protein folding, pHLIP has utility as an agent to target diseased tissues and translocate molecules through the membrane into the cytoplasm of cells in environments with elevated levels of extracellular acidity, as in cancer and inflammation. The results give the amount of energy that might be used to move cargo molecules across a membrane.thermodynamics ͉ drug delivery ͉ imaging ͉ membrane protein T he folding of helical membrane proteins can be conceptualized in terms of distinct steps: (i) peptide insertion and folding to form independently stable helices across a lipid bilayer, (ii) helix association to form a helix bundle intermediate, and (iii) further rearrangements of protein structure and/or binding of prosthetic groups to achieve a functional state (1). Insertion of most membrane proteins is facilitated in vivo by complex molecular machines, such as the translocon, which assist in placing hydrophobic sequences across the bilayer (2). In contrast to more hydrophobic sequences, moderately polar transmembrane domains of Cterminally-anchored proteins can postranslationally translocate themselves into membranes in a translocon-defective yeast strain (3, 4), seeking the free-energy minimum (5). Thus, insertion of a disordered peptide in aqueous solution to form a transbilayer ␣-helix is accompanied by a release of energy, so thermodynamic studies of the interaction of proteins and peptides with a lipid bilayer can provide insights regarding folding. However, such studies are significantly complicated by the poor solubility of membrane peptides, which has made it difficult to separate the contributions of peptide interactions with a lipid bilayer from self-interactions and aggregation.We have been studying a useful system for measurement of the thermodynamics and kinetics of peptide insertion and folding across a lipid bilayer. It is based on the pH low-insertion peptide (pHLIP), which has three major states: (I) soluble in water in an unstructured, monomeric state, (II) bound to the surface of a lipid bilayer in an unstructu...

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Shape variation of bilayer membrane daughter vesicles induced by anisotropic membrane inclusions

Cited by 9 publications

References 21 publications

Energetics Of Peptide (pHLIP) Binding To And Folding Across A Lipid Bilayer Membrane

Energetics Of Peptide (pHLIP) Binding To And Folding Across A Lipid Bilayer Membrane

Systems biology and physical biology of clathrin-mediated endocytosis

Energetics of peptide (pHLIP) binding to and folding across a lipid bilayer membrane

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