Spontaneous emulsification and self-propulsion of oil droplets induced by the synthesis of amino acid-based surfactants.

It is well known that oil droplets in or on water exhibit spontaneous movement induced by surfactants, and this self-propulsion is regarded as an important factor in droplet-based models for a living cell. We report here an oil-droplet system spontaneously producing amino acid-based surfactants, which are then utilized for the droplets' self-propulsion. Thus this system is an active system capable of producing the fuel for the propulsion by itself, which can be used as a conceptual model for cell metabolism.

Self-inverted reciprocation of an oil droplet on a surfactant solution.

Self-motion of an oil droplet was investigated on a sodium dodecyl sulfate (SDS) aqueous phase. With an increase in the concentration of SDS, the nature of self-motion of a butyl salicylate (BS) droplet as the oil droplet was changed, i.e., no motion, reciprocation with a small amplitude, and reciprocation with a large amplitude, which was a value close to the half-length of the chamber. The interfacial tension, contact angle, and convective flow around the droplet were measured to clarify the driving force of reciprocation. The mechanisms of two types of reciprocation and mode-change were discussed in terms of the adsorption of SDS molecules at the BS/water interface and the dissolution of a mixture of BS and SDS into the bulk phase, the convective flow, and the Young's equation. The features of reciprocation and mode-change depending on the concentration of SDS were qualitatively reproduced by numerical calculation based on an equation of motion and the kinetics of SDS and BS at the air/aqueous interface.

Spontaneous change in trajectory patterns of a self-propelled oil droplet at the air-surfactant solution interface.

Trajectory-pattern formation of a self-propelled oil droplet floating on the surface of a surfactant solution in a circular dish is studied both experimentally and by simulation. The Marangoni effect induced by the dissolution of oil in the solution drives the droplet's motion. The trajectories spontaneously organize into several patterns including circular, knot-forming, back-and-forth, and irregular ones. They are either global patterns, whose center corresponds to the dish center, or other local patterns. Our simple model consisting of three forces, the driving force, the viscous resistance, and the repulsion from the boundary, successfully reproduces the global trajectory patterns including the power spectrum of the droplet speed.

Finger-like pattern formation in dilute surfactant pentaethylene glycol monododecyl ether solutions.

We report here peculiar finger-like patterns observed during the phase separation process of dilute micellar pentaethylene glycol monododecyl ether solutions. The patterns were composed of parallel and periodic threads of micelle-rich domains. Prior to this pattern formation, the phase separation always started with the appearance of water-rich domains rimmed by the micelle-rich domains. It was found that these rims played a significant role in the pattern formation. We explain this pattern formation using a simple simulation model with disconnectable springs. The simulation results suggested that the spatially inhomogeneous elasticity or connectivity of a transient gel of worm-like micelles was responsible for the rim formation. The rims thus formed lead rim-induced nucleation, growth, and elongation of the domains owing to their small mobility and the elastic frustration around them. These rim-induced processes eventually produce the observed finger-like patterns.

An Insight into the pathway of the amyloid fibril formation of hen egg white lysozyme obtained from a small-angle X-ray and neutron scattering study.

It is known that hen egg white lysozyme (HEWL) forms amyloid fibrils. Since HEWL is one of the proteins that have been studied most extensively and is closely related to human lysozyme, the variants of which form the amyloid fibrils that are related to hereditary systemic amyloidosis, this protein is an ideal model to study the mechanism of amyloid fibril formation. In order to gain an insight into the mechanism of amyloid fibril formation, systematic and detailed studies to detect and characterize various structural states of HEWL were conducted. Since HEWL forms amyloid fibrils in highly concentrated ethanol solutions, solutions of various concentrations of HEWL in various concentrations of ethanol were prepared, and the structures of HEWL in these solutions were investigated by small-angle X-ray and neutron scattering. It was shown that the structural states of HEWL were distinguished as the monomer state, the state of the dimer formation, the state of the protofilament formation, the protofilament state, and the state towards the formation of amyloid fibrils. A phase diagram of these structural states was obtained as a function of protein, water and ethanol concentrations. It was found that under the monomer state the structural changes of HEWL were not gross changes in shape but local conformational changes, and the dimers, formed by the association at the end of the long axis of HEWL, had an elongated shape. Circular dichroism measurements showed that the large changes in the secondary structures of HEWL occurred during dimer formation. The protofilaments were formed by stacking of the dimers with their long axis (nearly) perpendicular to and rotated around the protofilament axis to form a helical structure. These protofilaments were characterized by their radius of gyration of the cross-section of 2.4nm and the mass per unit length of 16,000(+/-2300)Da/nm. It was shown that the changes of the structural states towards the amyloid fibril formation occurred via lateral association of the protofilaments. A pathway of the amyloid fibril formation of HEWL was proposed from these results.