RESUMO
We report a chemically driven membrane shape instability that triggers the ejection of a tubule growing exponentially toward a chemical source. The instability is initiated by a dilation of the exposed monolayer, which is coupled to the membrane spontaneous curvature and slowed down by intermonolayer friction. Our experiments are performed by local delivery of a basic pH solution to a giant vesicle. Quantitative fits of the data give an intermonolayer friction coefficient b approximately 2x10;{9} J s/m;{4}. The exponential growth of the tubule may be explained by a Marangoni stress yielding a pulling force proportional to its length.
Assuntos
Bicamadas Lipídicas/química , Lipídeos/química , Modelos Químicos , Lipossomas Unilamelares/química , Membrana Celular/química , Concentração de Íons de Hidrogênio , TermodinâmicaRESUMO
We examine the time-dependent distortion of a nearly circular viscous domain in an infinite viscous sheet when suction occurs. Suction, the driving force of the instability, can occur everywhere in the two phases separated by an interface. The model assumes a two-dimensional Stokes flow; the selection of the wavelength at short times is determined by a variational procedure. Contrary to the viscous fingering instability, undulations of the boundary may be observed for enough pumping, whatever the sign of the viscosity contrast between the two fluids involved. We apply our model to the suction by lipoproteins of cholesterol-enriched domains in giant unilamellar vesicles. Comparison of the number of undulations given by the model and by the experiments gives reasonable values of physical quantities such as the viscosities of the domains.
RESUMO
The adsorption of beta-casein at the air-solution interface has been monitored in equilibrium conditions by neutron reflectivity. It was observed that for a bulk concentration of 100 mg/L, the amount of protein adsorbed per unit surface increases from 2.8 to 4.4 mg/m2 when the ethanol concentration in the bulk changes from 0 to 20% (v/v). Surface pressure measurements on aqueous solutions indicate that the surface pressure is higher when both protein and alcohol are added than when a single substance is in the solution. The addition of protein has an effect when the alcohol concentration is less than 20%. These results are consistent with the occurrence at the interface of a protein network leaving a surface fraction available for ethanol. A thermodynamic model has been developed using scaling law arguments to model the surface pressure and dilational modulus measurements. It introduces an exponent which is characteristic of the solvent "quality" and of the structure of the interfacial layer. The results are interpreted as showing that ethanol modifies the solvent properties, the interactions between the protein and the solvent, and the structure of the adsorption layer. The main transition seems to occurr at 6% ethanol. Copyright 1998 Academic Press.