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1.
Biophys J ; 113(5): 1072-1079, 2017 Sep 05.
Artigo em Inglês | MEDLINE | ID: mdl-28877490

RESUMO

Actin is one of the main components of the architecture of cells. Actin filaments form different polymer networks with versatile mechanical properties that depend on their spatial organization and the presence of cross-linkers. Here, we investigate the mechanical properties of actin bundles in the absence of cross-linkers. Bundles are polymerized from the surface of mDia1-coated latex beads, and deformed by manipulating both ends through attached beads held by optical tweezers, allowing us to record the applied force. Bundle properties are strikingly different from the ones of a homogeneous isotropic beam. Successive compression and extension leads to a decrease in the buckling force that we attribute to the bundle remaining slightly curved after the first deformation. Furthermore, we find that the bundle is solid, and stiff to bending, along the long axis, whereas it has a liquid and viscous behavior in the transverse direction. Interpretation of the force curves using a Maxwell visco-elastic model allows us to extract the bundle mechanical parameters and confirms that the bundle is composed of weakly coupled filaments. At short times, the bundle behaves as an elastic material, whereas at long times, filaments flow in the longitudinal direction, leading to bundle restructuring. Deviations from the model reveal a complex adaptive rheological behavior of bundles. Indeed, when allowed to anneal between phases of compression and extension, the bundle reinforces. Moreover, we find that the characteristic visco-elastic time is inversely proportional to the compression speed. Actin bundles are therefore not simple force transmitters, but instead, complex mechano-transducers that adjust their mechanics to external stimulation. In cells, where actin bundles are mechanical sensors, this property could contribute to their adaptability.


Assuntos
Actinas/metabolismo , Actinas/química , Adaptação Fisiológica , Fenômenos Biomecânicos , Elasticidade , Modelos Moleculares , Pinças Ópticas , Reologia , Estresse Mecânico , Viscosidade
2.
Traffic ; 11(12): 1519-29, 2010 Dec.
Artigo em Inglês | MEDLINE | ID: mdl-20887377

RESUMO

To maintain cell membrane homeostasis, lipids must be dynamically redistributed during the formation of transport intermediates, but the mechanisms driving lipid sorting are not yet fully understood. Lowering sphingolipid concentration can reduce the bending energy of a membrane, and this effect could account for sphingolipid depletion along the retrograde pathway. However, sphingolipids and cholesterol are enriched along the anterograde pathway, implying that other lipid sorting mechanisms, such as protein-mediated sorting, can dominate. To characterize the influence of protein binding on the lipid composition of highly curved membranes, we studied the interactions of the B-subunit of Shiga toxin (STxB) with giant unilamellar vesicles containing its glycosphingolipid receptor [globotriaosylceramide (Gb3)]. STxB binding induced the formation of tubular membrane invaginations, and fluorescence microscopy images of these highly curved membranes were consistent with co-enrichment of Gb3 and sphingolipids. In agreement with theory, sorting was stronger for membrane compositions close to demixing. These results strongly support the hypothesis that proteins can indirectly mediate the sorting of lipids into highly curved transport intermediates via interactions between lipids and the membrane receptor of the protein.


Assuntos
Membrana Celular/metabolismo , Metabolismo dos Lipídeos , Toxina Shiga/metabolismo , Esfingolipídeos/metabolismo , Triexosilceramidas/metabolismo , Animais , Transporte Biológico , Membrana Celular/química , Humanos , Ligação Proteica , Toxina Shiga/química , Esfingolipídeos/química , Triexosilceramidas/química , Lipossomas Unilamelares/química , Lipossomas Unilamelares/metabolismo
3.
Chemphyschem ; 10(1): 222-5, 2009 Jan 12.
Artigo em Inglês | MEDLINE | ID: mdl-19072821

RESUMO

Herein, we study the viscoelastic response of concentrated salt solutions using surface waves excited by electrocapillarity. We show that the hydrodynamic behaviour of the solutions is similar to that of water at concentrations up to 2 m-well above the concentration C*, at which inhibition of bubble coalescence occurs in these solutions. This result excludes the occurrence of changes in the slip conditions at C*, postulated to explain this inhibition. Our study is carried out on salts that both increase and decrease the surface tension. We observe that the salt that decreases the tension does not change the surface behaviour at all, whereas the other two salts essentially produce negative contributions to the surface viscoelasticity at very high salt concentrations. The effects observed are quite large and remain to be explained.


Assuntos
Eletrólitos/química , Substâncias Viscoelásticas/química , Algoritmos , Tensão Superficial
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