The mechanical response of giant liposomes to compression between two parallel plates is investigated in the context of an artificial actin cortex adjacent to the inner leaflet of the bilayer. We found that nonlinear membrane theory neglecting the impact of bending sufficiently describes the mechanical response of liposomes consisting of fluid lipids to compression whereas the formation of an actin cortex or the use of gel-phase lipids generally leads to substantial stiffening of the shell. Giant vesicles are gently adsorbed on glassy surfaces and are compressed with tipless cantilevers using an atomic force microscope. Force-compression curves display a nonlinear response that allows us to determine the membrane tension σ0 and the area compressibility modulus K(A) by computing the contour of the vesicle as a function of the compression depth. The values for KA of fluid membranes correspond well to what is known from micropipet-suction experiments and computed from monitoring membrane undulations. The presence of a thick actin shell adjacent to the inner leaflet of the liposome membrane stiffens the system considerably, as mirrored in a significantly higher apparent area compressibility modulus.
Indentation of giant liposomes with a conical indenter is described by means of a tension-based membrane model. We found that nonlinear membrane theory neglecting the impact of bending sufficiently describes the mechanical response of liposomes to indentation as measured by atomic force microscopy. Giant vesicles are gently adsorbed on glassy surfaces via avidin-biotin linkages and indented centrally using an atomic force microscope equipped with conventional sharp tips mounted on top of an inverted microscope. Force indentation curves display a nonlinear response that allows to extract pre-stress of the bilayer T0 and the area compressibility modulus KA by computing the contour of the vesicle at a given force. The values for KA of fluid membranes correspond well to what is known from micropipet suction experiments and inferred from membrane undulation monitoring. Assembly of actin shells inside the liposome considerably stiffens the vesicles resulting in significantly larger area compressibility modules. The analysis can be easily extended to different indenter geometries with rotational symmetry.
Chemotactic responses of Dictyostelium discoideum cells to periodic self-generated signals of extracellular cAMP comprise a large number of intricate morphological changes on different length scales. Here, we scrutinized chemotaxis of single Dictyostelium discoideum cells under conditions of starvation using a variety of optical, electrical and acoustic methods. Amebas were seeded on gold electrodes displaying impedance oscillations that were simultaneously analyzed by optical video microscopy to relate synchronous changes in cell density, morphology, and distance from the surface to the transient impedance signal. We found that starved amebas periodically reduce their overall distance from the surface producing a larger impedance and higher total fluorescence intensity in total internal reflection fluorescence microscopy. Therefore, we propose that the dominant sources of the observed impedance oscillations observed on electric cell-substrate impedance sensing electrodes are periodic changes of the overall cell-substrate distance of a cell. These synchronous changes of the cell-electrode distance were also observed in the oscillating signal of acoustic resonators covered with amebas. We also found that periodic cell-cell aggregation into transient clusters correlates with changes in the cell-substrate distance and might also contribute to the impedance signal. It turned out that cell-cell contacts as well as cell-substrate contacts form synchronously during chemotaxis of Dictyostelium discoideum cells.
A sheep in wolf's clothes? Mimicking the crucial conformational step in viral fusion promises to be an efficient method to detect potential antagonists of retroviral infection (see scheme). Reconstituted lipopeptides derived from the N peptides of the class I virus fusion protein of SIV serve as receptors for potential inhibitors that function like the C peptides of the virus protein.
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