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1.
Phys Rev Lett ; 124(3): 038001, 2020 Jan 24.
Artigo em Inglês | MEDLINE | ID: mdl-32031854

RESUMO

Cholesterol is a crucial component of mammalian cell membranes that takes part in many vital processes. It is generally accepted that cholesterol stabilizes the membrane and induces transitions into ordered states. In contrast to expectations, we demonstrate that cholesterol can destabilize the membrane by creating a nanodomain around a perpendicularly embedded ultrashort carbon nanotube (CNT), and we show that cholesterol triggers the translocation of an ultrashort CNT through the cell membrane. Using atomistic simulations, we report the existence of a nanoscale domain around an ultrashort carbon nanotube within a crossover distance of 0.9 nm from the surface of the nanotube, where the properties of the bilayer are different from the bulk: the domain is characterized by increased fluctuations, increased thickness, and increased order of the lipids with respect to the bulk. Cholesterol decreases the thickness and order of lipids and increases the fluctuations with respect to a pure lipid bilayer. Experimentally, we confirm that cholesterol nanodomains provoke spontaneous translocation of nanotubes through a lipid bilayer even for low membrane tensions. A specially designed microfluidic device allows us to trace the kinetic pathway of the translocation process and establish the threshold cholesterol concentration of 20% for translocation. The reported nanoscale cholesterol-induced membrane restructuring near the ultrashort CNT in lipid membranes enables precise control and specific targeting of a membrane using cholesterol. As an example, it may allow for specific targeting between cholesterol-rich mammalian cells and cholesterol-poor bacterial cells.


Assuntos
Membrana Celular/química , Colesterol/química , Lipídeos de Membrana/química , Modelos Químicos , Nanotubos de Carbono/química , Membrana Celular/metabolismo , Colesterol/metabolismo , Bicamadas Lipídicas/química , Bicamadas Lipídicas/metabolismo , Lipídeos de Membrana/metabolismo , Modelos Biológicos
2.
J Basic Microbiol ; 60(3): 207-215, 2020 Mar.
Artigo em Inglês | MEDLINE | ID: mdl-31960983

RESUMO

The treatment of Helicobacter pylori usually fails due to their ability to form biofilms and resistance to antibiotics. This might potentially lead to gastric carcinoma and mucosa-associated lymphoid tissue lymphoma. In the present study, we elucidate the potential role of N-acylhomoserine lactonase stabilized silver nanoparticles (AiiA-AgNPs) in treating biofilms produced by H. pylori. AiiA-AgNPs inhibited quorum sensing (QS) by degradation of QS molecules, thereby reducing biofilm formation, urease production, and altering cell surface hydrophobicity of H. pylori. AiiA-AgNPs showed no cytotoxic effects on RAW 264.7 macrophages at the effective concentration (1-5 µM) of antibiofilm activity. In addition, AiiA-AgNP in high concentration (80-100 µM) exhibited cytotoxicity against HCT-15 carcinoma cells, depicting its therapeutic role in treating cancer.


Assuntos
Antibacterianos/farmacologia , Biofilmes/efeitos dos fármacos , Hidrolases de Éster Carboxílico/farmacologia , Helicobacter pylori/efeitos dos fármacos , Percepção de Quorum/efeitos dos fármacos , Prata/farmacologia , Animais , Antibacterianos/química , Antineoplásicos/química , Antineoplásicos/farmacologia , Biofilmes/crescimento & desenvolvimento , Hidrolases de Éster Carboxílico/química , Linhagem Celular Tumoral , Membrana Celular/química , Membrana Celular/efeitos dos fármacos , Sobrevivência Celular/efeitos dos fármacos , Helicobacter pylori/metabolismo , Humanos , Interações Hidrofóbicas e Hidrofílicas/efeitos dos fármacos , Nanopartículas Metálicas/química , Camundongos , Células RAW 264.7 , Prata/química , Urease/metabolismo
3.
Biomed Chromatogr ; 34(2): e4763, 2020 Feb.
Artigo em Inglês | MEDLINE | ID: mdl-31770450

RESUMO

Target biomolecule-immobilized magnetic beads could be used as a powerful tool for screening active compounds present in natural products. Low damage rates of the target proteins, associated with the availability of diverse automated online approaches for analysis, make it a valuable tool for affinity studies. RAW264.7 cells (a kind of murine macrophage cell line) were used in this study. These cellular membranes were immobilized onto the surface of MBs and were used for screening the active compounds of Polygonatum sibiricum. Combining this technique with HPLC led to the identification of an active compound and its biological activity was confirmed. This is the first report establishing the use of RAW264.7 cellular membrane-coated magnetic bead fishing followed by HPLC analysis for screening active compounds from natural products.


Assuntos
Membrana Celular/química , Cromatografia Líquida de Alta Pressão/métodos , Imãs/química , Extratos Vegetais , Polygonatum/química , Animais , Membrana Celular/metabolismo , Descoberta de Drogas , Camundongos , Compostos Fitoquímicos , Extratos Vegetais/análise , Extratos Vegetais/química , Extratos Vegetais/isolamento & purificação , Extratos Vegetais/metabolismo , Células RAW 264.7
4.
Chemphyschem ; 21(1): 9-12, 2020 Jan 03.
Artigo em Inglês | MEDLINE | ID: mdl-31483076

RESUMO

Whilst the formation of plastic nanoparticles (nanoplastics) from plastic wastes has been unequivocally evidenced, little is known about the effects of these materials on living organisms at the subcellular or molecular levels. In the present contribution we show through molecular dynamics simulations that polyethylene nanoparticles dissolve in the hydrophobic core of lipid bilayers into a network of disentangled, single polymeric chains. The thereby induced structural and dynamic changes in the bilayer alter vital functions of the cell membrane, which if lacking a mechanism to decompose the polymer chains may result in the death of the cell.


Assuntos
Membrana Celular/química , Bicamadas Lipídicas/química , Nanopartículas/química , Polietileno/química , Interações Hidrofóbicas e Hidrofílicas , Simulação de Dinâmica Molecular
5.
Chem Commun (Camb) ; 56(4): 547-550, 2020 Jan 14.
Artigo em Inglês | MEDLINE | ID: mdl-31829350

RESUMO

We report a cancer cell membrane-camouflaged nanoreactor based on a GOx decorated TiO2@MnO2 core-shell structure for enhanced radiotherapy against cancer metastasis. The nanoreactor could specifically target tumor tissues, catalytically oxidize glucose to generate H2O2, and generate abundant ROS under X-ray irradiation.


Assuntos
Neoplasias da Mama/radioterapia , Neoplasias da Mama/secundário , Membrana Celular/efeitos dos fármacos , Compostos de Manganês/farmacologia , Melanoma/radioterapia , Melanoma/secundário , Nanopartículas/química , Óxidos/farmacologia , Titânio/farmacologia , Animais , Neoplasias da Mama/patologia , Linhagem Celular Tumoral , Membrana Celular/química , Sobrevivência Celular/efeitos dos fármacos , Feminino , Compostos de Manganês/química , Melanoma/patologia , Camundongos , Óxidos/química , Tamanho da Partícula , Propriedades de Superfície , Titânio/química , Raios X
6.
Artigo em Inglês | MEDLINE | ID: mdl-31841981

RESUMO

There is a great need for high-throughput protein purification to produce protein molecules for research and therapeutics. Although there have been significant advancements made in automated multi-step chromatography and preparative in-process design-of-experiment (DOE) capabilities in commercial fast performance liquid chromatography (FPLC) instruments, almost all commercial FPLCs rely on a binary buffer mixing system, which hinders automated buffer preparation. Nevertheless, current-generation FPLCs are equipped with a quaternary mixer designed for limited in-line buffer preparation and preparative pH scouting DOE experiments. We decided to leverage the quaternary mixing capability by extending and re-programming AkTA Avant's quaternary valve into an automated in-process buffer preparation system to simplify automated purification requiring complex washing steps. We accomplished this by using two extra inlet valves, a sample valve, and versatile valve to split inputs of the quaternary valve into software-selectable stock solutions of pH buffers, salts, eluents, and additives. We also devised a new flow scheme to perform automated two-step chromatography using only one versatile valve. This was accomplished by using only stock parts and software to facilitate reproduction. To demonstrate the versatility and capability of the system, we purified a transmembrane protein that requires a detergent to stay soluble and needs an in-column, high-salt washing step to achieve high purity.


Assuntos
Automação Laboratorial/instrumentação , Membrana Celular/química , Cromatografia Líquida/instrumentação , Proteínas de Membrana/isolamento & purificação , Tampões (Química) , Cromatografia Líquida/métodos , Desenho de Equipamento , Humanos
7.
Chemistry ; 26(7): 1511-1517, 2020 Feb 03.
Artigo em Inglês | MEDLINE | ID: mdl-31867761

RESUMO

Solid-state 19 F NMR is a powerful method to study the interactions of biologically active peptides with membranes. So far, in labelled peptides, the 19 F-reporter group has always been installed on the side chain of an amino acid. Given the fact that monofluoroalkenes are non-hydrolyzable peptide bond mimics, we have synthesized a monofluoroalkene-based dipeptide isostere, Val-Ψ[(Z)-CF=CH]-Gly, and inserted it in the sequence of two well-studied antimicrobial peptides: PGLa and (KIGAKI)3 are representatives of an α-helix and a ß-sheet. The conformations and biological activities of these labeled peptides were studied to assess the suitability of monofluoroalkenes for 19 F NMR structure analysis.


Assuntos
Alcenos/química , Peptídeos Catiônicos Antimicrobianos/química , Membrana Celular/química , Espectroscopia de Ressonância Magnética , Sequência de Aminoácidos , Peptídeos Catiônicos Antimicrobianos/síntese química , Flúor/química , Conformação Proteica em alfa-Hélice , Coloração e Rotulagem/métodos
8.
Phys Rev Lett ; 123(22): 228102, 2019 Nov 29.
Artigo em Inglês | MEDLINE | ID: mdl-31868410

RESUMO

Biological function requires cell-cell adhesions to tune their cohesiveness; for instance, during the opening of new fluid-filled cavities under hydraulic pressure. To understand the physical mechanisms supporting this adaptability, we develop a stochastic model for the hydraulic fracture of adhesive interfaces bridged by molecular bonds. We find that surface tension strongly enhances the stability of these interfaces by controlling flaw sensitivity, lifetime, and optimal architecture in terms of bond clustering. We also show that bond mobility embrittles adhesions and changes the mechanism of decohesion. Our study provides a mechanistic background to understand the biological regulation of cell-cell cohesion and fracture.


Assuntos
Adesão Celular/fisiologia , Junções Intercelulares/química , Junções Intercelulares/fisiologia , Modelos Biológicos , Membrana Celular/química , Membrana Celular/fisiologia , Simulação por Computador , Processos Estocásticos , Tensão Superficial
9.
Mol Biol (Mosk) ; 53(6): 968-981, 2019.
Artigo em Russo | MEDLINE | ID: mdl-31876276

RESUMO

This review summarizes the main achievements of recent years in molecular organization research of yeast cell surface, i.e., the compartment that consists of the coordinately functioning plasma membrane, periplasmic space, and cell wall. There are data on vesicular transport to the external environment through the cell wall and the formation of channels in the wall, which indicate the possibility of dynamic rearrangements of the molecular structure of the yeast cell wall. There is an idea about the mosaic arrangement of the compartments of the plasma membrane. The hypothesis has been suggested on the heterogeneity of the molecular structure of the cell wall, which is usually considered as uniform except for the budding zones. The groups of proteins that form the molecular assembly of the yeast cell surface have been described. Special attention has been paid for proteins with amyloid properties, including Bgl2p glucanosyltransglycosylase, which is important for virulence in pathogenic yeast, and Gas1p, the first of the studied proteins of the cell surface, which is involved in the regulation of ribosomal DNA transcriptional silencing. The data on the structure of receptors localized on the cell surface and the "moonlight" proteins, involved in the cell stress response of yeasts, have been given.


Assuntos
Membrana Celular/metabolismo , Parede Celular/metabolismo , Periplasma/metabolismo , Saccharomyces cerevisiae/citologia , Saccharomyces cerevisiae/metabolismo , Amiloide/química , Amiloide/metabolismo , Membrana Celular/química , Parede Celular/química , Periplasma/química , Proteínas de Saccharomyces cerevisiae/química , Proteínas de Saccharomyces cerevisiae/metabolismo
10.
Chem Commun (Camb) ; 55(96): 14446-14449, 2019 Nov 28.
Artigo em Inglês | MEDLINE | ID: mdl-31724658

RESUMO

A rational design of a benzoperylene probe BP-3 with positive charge allows for turn-on excimer emission, and wash-free cell membrane imaging. BP-3 possesses excellent chemical, thermal and photo stability. And the Stokes shift of the excimer emission is considerably large (90-100 nm), which very much avoids the background fluorescence interference.


Assuntos
Membrana Celular/química , Corantes Fluorescentes/química , Perileno/análogos & derivados , Humanos , Células MCF-7 , Microscopia Confocal , Perileno/química , Solventes , Espectrometria de Fluorescência
11.
Org Biomol Chem ; 17(45): 9693-9697, 2019 12 07.
Artigo em Inglês | MEDLINE | ID: mdl-31691700

RESUMO

A series of cyclic Arg-rich mitochondria-penetrating peptides were prepared with variation in the macrocycle size and the chirality of Arg residues. A cyclic heptapeptide was demonstrated to be an efficient mitochondria-specific delivery vector for delivering membrane impermeable peptides.


Assuntos
Membrana Celular/metabolismo , Peptídeos Penetradores de Células/metabolismo , Mitocôndrias/metabolismo , Membrana Celular/química , Sobrevivência Celular , Peptídeos Penetradores de Células/química , Ciclização , Células HeLa , Humanos , Mitocôndrias/química , Conformação Molecular
12.
Nat Commun ; 10(1): 4526, 2019 10 04.
Artigo em Inglês | MEDLINE | ID: mdl-31586057

RESUMO

Genetically encoded probes monitoring H2O2 fluctuations in living organisms are key to decipher redox signaling events. Here we use a new probe, roGFP2-Tpx1.C169S, to monitor pre-toxic fluctuations of peroxides in fission yeast, where the concentrations linked to signaling or to toxicity have been established. This probe is able to detect nanomolar fluctuations of intracellular H2O2 caused by extracellular peroxides; expression of human aquaporin 8 channels H2O2 entry into fission yeast decreasing membrane gradients. The probe also detects H2O2 bursts from mitochondria after addition of electron transport chain inhibitors, the extent of probe oxidation being proportional to the mitochondrial activity. The oxidation of this probe is an indicator of steady-state levels of H2O2 in different genetic backgrounds. Metabolic reprogramming during growth in low-glucose media causes probe reduction due to the activation of antioxidant cascades. We demonstrate how peroxiredoxin-based probes can be used to monitor physiological H2O2 fluctuations.


Assuntos
Citosol/química , Peróxido de Hidrogênio/análise , Técnicas de Sonda Molecular , Peroxirredoxinas/química , Membrana Celular/química , Genes Reporter , Peróxido de Hidrogênio/química , Proteínas Luminescentes/química , Proteínas Luminescentes/genética , Mitocôndrias/química , Sondas Moleculares/química , Oxirredução , Engenharia de Proteínas , Schizosaccharomyces
13.
Chem Commun (Camb) ; 55(87): 13074-13077, 2019 Oct 29.
Artigo em Inglês | MEDLINE | ID: mdl-31588930

RESUMO

In this study, we report the first synthesis of an alkyne-based trehalose monomycolate probe containing a ß-hydroxylated fatty acid and an α-branched chain similar to those of the natural mycolic acid. We demonstrate its utility for the labeling of the mycomembrane of Corynebacteria as well as for the study of mycoloyltransferases.


Assuntos
Aciltransferases/análise , Membrana Celular/química , Corynebacterium/enzimologia , Corantes Fluorescentes/química , Ácidos Micólicos/química , Aciltransferases/metabolismo , Membrana Celular/metabolismo , Corynebacterium/citologia , Corantes Fluorescentes/síntese química , Estrutura Molecular , Ácidos Micólicos/síntese química
14.
J Chem Theory Comput ; 15(11): 6444-6455, 2019 Nov 12.
Artigo em Inglês | MEDLINE | ID: mdl-31593632

RESUMO

Integral membrane proteins are ubiquitous in biological cellular and subcellular membranes. Despite their significance to cell function, isolation of membrane proteins from their hydrophobic lipid environment and further characterization remains a challenge. To obtain insights into membrane proteins, computational approaches such as docking or self-assembly simulations have been used; however, the promise of these approaches has been limited due to the computational cost. Here we present a new approach called Protein AssociatioN Energy Landscape (PANEL) that provides an extensive and converged data set for all possible conformations of membrane protein associations using a combination of stochastic sampling and equilibration simulations. The PANEL method samples the rotational space around both interacting proteins to obtain the comprehensive interaction energy landscape. We demonstrate the versatility of the PANEL method using two distinct applications: (a) dimerization of claudin-5 tight junction proteins in phospholipid bilayer membrane and (b) dimer and trimer formation of the Outer membrane protein F (OmpF) in the lipopolysaccharide-rich bacterial outer membrane. Both applications required only a fraction of simulation cost compared to self-assembly simulations. The method is robust as it can capture changes in protein-protein conformations caused by point mutations. Moreover, the method is versatile and independent of the molecular resolution (atomistic or coarse grain) or the choice of force field employed to compute the pair-interaction energies. The PANEL method is implemented in easy-to-use scripts that are available for download for general use by the scientific community to characterize any pair of interacting integral membrane proteins.


Assuntos
Proteínas de Membrana/química , Modelos Moleculares , Bactérias/metabolismo , Membrana Celular/química , Membrana Celular/metabolismo , Dimerização , Proteínas de Membrana/metabolismo , Mutação Puntual , Porinas/química , Porinas/genética , Porinas/metabolismo , Conformação Proteica , Termodinâmica
15.
J Chem Phys ; 151(15): 154103, 2019 Oct 21.
Artigo em Inglês | MEDLINE | ID: mdl-31640367

RESUMO

We study diffusion of particles on the surface of a sphere toward a partially reactive circular target with partly reversible binding kinetics. We solve the coupled diffusion-reaction equations and obtain the exact expressions for the time-dependent concentration of particles and the total diffusive flux. Explicit asymptotic formulas are derived in the small target limit. This study reveals the strong effects of reversible binding kinetics onto diffusion-mediated reactions that may be relevant for many biochemical reactions on cell membranes.


Assuntos
Difusão , Modelos Químicos , Membrana Celular/química , Cinética , Propriedades de Superfície
16.
Mol Cell ; 76(2): 295-305, 2019 10 17.
Artigo em Inglês | MEDLINE | ID: mdl-31604601

RESUMO

Biomolecular condensation is emerging as an essential process for cellular compartmentalization. The formation of biomolecular condensates can be driven by liquid-liquid phase separation, which arises from weak, multivalent interactions among proteins and nucleic acids. A substantial body of recent work has revealed that diverse cellular processes rely on biomolecular condensation and that aberrant phase separation may cause disease. Many proteins display an intrinsic propensity to undergo phase separation. However, the mechanisms by which cells regulate phase separation to build functional condensates at the appropriate time and location are only beginning to be understood. Here, we review three key cellular mechanisms that enable the control of biomolecular phase separation: membrane surfaces, post-translational modifications, and active processes. We discuss how these mechanisms may function in concert to provide robust control over biomolecular condensates and suggest new research avenues that will elucidate how cells build and maintain these key centers of cellular compartmentalization.


Assuntos
Compartimento Celular , Membrana Celular/metabolismo , Ácidos Nucleicos/metabolismo , Processamento de Proteína Pós-Traducional , Transporte Proteico , Proteínas/metabolismo , Animais , Membrana Celular/química , Endocitose , Humanos , Membranas Intracelulares/metabolismo , Chaperonas Moleculares/metabolismo , Conformação de Ácido Nucleico , Ácidos Nucleicos/química , Conformação Proteica , Proteínas/química , Solubilidade , Relação Estrutura-Atividade
17.
Nat Protoc ; 14(11): 3183-3204, 2019 11.
Artigo em Inglês | MEDLINE | ID: mdl-31605097

RESUMO

Biological membranes define the boundaries of cells and are composed primarily of phospholipids and membrane proteins. It has become increasingly evident that direct interactions of membrane proteins with their surrounding lipids play key roles in regulating both protein conformations and function. However, the exact nature and structural consequences of these interactions remain difficult to track at the molecular level. Here, we present a protocol that specifically addresses this challenge. First, hydrogen-deuterium exchange mass spectrometry (HDX-MS) of membrane proteins incorporated into nanodiscs of controlled lipid composition is used to obtain information on the lipid species that are involved in modulating the conformational changes in the membrane protein. Then molecular dynamics (MD) simulations in lipid bilayers are used to pinpoint likely lipid-protein interactions, which can be tested experimentally using HDX-MS. By bringing together the MD predictions with the conformational readouts from HDX-MS, we have uncovered key lipid-protein interactions implicated in stabilizing important functional conformations. This protocol can be applied to virtually any integral membrane protein amenable to classic biophysical studies and for which a near-atomic-resolution structure or homology model is available. This protocol takes ~4 d to complete, excluding the time for data analysis and MD simulations, which depends on the size of the protein under investigation.


Assuntos
Membrana Celular/química , Bicamadas Lipídicas/química , Proteínas de Membrana/química , Medição da Troca de Deutério , Espectrometria de Massas , Simulação de Dinâmica Molecular , Conformação Proteica
18.
Nat Commun ; 10(1): 4763, 2019 10 18.
Artigo em Inglês | MEDLINE | ID: mdl-31628328

RESUMO

Phagocytosis is a cellular process for internalization of micron-sized large particles including pathogens. The Bin-Amphiphysin-Rvs167 (BAR) domain proteins, including the FCH-BAR (F-BAR) domain proteins, impose specific morphologies on lipid membranes. Most BAR domain proteins are thought to form membrane invaginations or protrusions by assembling into helical submicron-diameter filaments, such as on clathrin-coated pits, caveolae, and filopodia. However, the mechanism by which BAR domain proteins assemble into micron-scale phagocytic cups was unclear. Here, we show that the two-dimensional sheet-like assembly of Growth Arrest-Specific 7 (GAS7) plays a critical role in phagocytic cup formation in macrophages. GAS7 has the F-BAR domain that possesses unique hydrophilic loops for two-dimensional sheet formation on flat membranes. Super-resolution microscopy reveals the similar assemblies of GAS7 on phagocytic cups and liposomes. The mutations of the loops abolishes both the membrane localization of GAS7 and phagocytosis. Thus, the sheet-like assembly of GAS7 plays a significant role in phagocytosis.


Assuntos
Macrófagos/metabolismo , Lipídeos de Membrana/metabolismo , Proteínas do Tecido Nervoso/metabolismo , Fagocitose , Sequência de Aminoácidos , Animais , Membrana Celular/química , Membrana Celular/metabolismo , Membrana Celular/ultraestrutura , Células HeLa , Humanos , Lipídeos de Membrana/química , Camundongos , Microscopia Eletrônica , Microscopia de Fluorescência , Modelos Moleculares , Mutação , Proteínas do Tecido Nervoso/química , Proteínas do Tecido Nervoso/genética , Domínios Proteicos , Isoformas de Proteínas/química , Isoformas de Proteínas/genética , Isoformas de Proteínas/metabolismo , Células RAW 264.7 , Homologia de Sequência de Aminoácidos
19.
J Chem Theory Comput ; 15(11): 6411-6421, 2019 Nov 12.
Artigo em Inglês | MEDLINE | ID: mdl-31564100

RESUMO

Advances in simulation methodologies, code efficiency, and computing power have enabled larger, longer, and more-complicated biological membrane simulations. The resulting membranes can be highly complex and have curved geometries that greatly deviate from a simple planar state. Studying these membranes requires appropriate characterization of geometric and topological properties of the membrane surface before any local lipid properties, such as areas and curvatures, can be computed. We present MemSurfer, an efficient and versatile tool to robustly compute membrane surfaces for a wide variety of large-scale molecular simulations. MemSurfer works independent of the type of simulation and directly on 3D point coordinates. As a result, MemSurfer can handle a variety of membranes. Using Delaunay triangulations and surface parameterizations, MemSurfer not only computes common lipid properties of interest but also provides direct access to the membrane surface itself, allowing the user to potentially conceive and compute a variety of nonstandard properties. The software provides a simple-to-use Python API and is released open-source under a GPL3 license.


Assuntos
Membrana Celular/química , Simulação de Dinâmica Molecular , Software , Animais , Bicamadas Lipídicas/química
20.
Phys Rev E ; 100(2-1): 022416, 2019 Aug.
Artigo em Inglês | MEDLINE | ID: mdl-31574724

RESUMO

One of the most widely used methods for determination of the bending elasticity modulus of model lipid membranes is the analysis of the shape fluctuations of nearly spherical lipid vesicles. The theoretical basis of this analysis is given by Milner and Safran [Phys. Rev. A 36, 4371 (1987)0556-279110.1103/PhysRevA.36.4371]. In their theory the stretching effects are not considered. In the present study we generalized their approach including the stretching effects deduced after application of the statistical mechanics to vesicles.


Assuntos
Membrana Celular/química , Elasticidade , Bicamadas Lipídicas/química , Temperatura Ambiente , Modelos Moleculares , Tensão Superficial
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