Twisting and buckling: a new undulation mechanism for artificial swimmers.

Among the various locomotion strategies of the animal kingdom, the undulation locomotion is of particular interest for biomimetic applications. In this paper, we present an artificial swimmer set into motion by a new and non-trivial undulation mechanism, based on the twisting and buckling of its body. The swimmer consists of a long cylinder of ferrogel which is polarized transversely and in opposite directions at each extremity. When it is placed on a water film and submitted to a transverse oscillating magnetic field, the worm-like swimmer undulates and swims. Whereas symmetry breaking is due to the field gradient, the undulations of the worm result from a torsional buckling instability as the polarized ends tend to align with the applied magnetic field. The critical magnetic field above which buckling and subsequent swimming is observed may be predicted using elasticity equations including the effect of the magnetic torque. As the length of the worm is varied, several undulation modes are observed which are in good agreement with the bending modes of an elastic rod with free ends.

Urea denaturation of alpha-hemolysin pore inserted in planar lipid bilayer detected by single nanopore recording: loss of structural asymmetry.

The aim of this work is to study pore protein denaturation inside a lipid bilayer and to probe current asymmetry as a function of the channel conformation. We describe the urea denaturation of alpha-hemolysin channel and the channel formation of alpha-hemolysin monomer incubated with urea prior to insertion into a lipid bilayer. Analysis of single-channel recordings of current traces reveals a sigmoid curve of current intensity as a function of urea concentration. The normalized current asymmetry at 29+/-4% is observed between 0 and 3.56M concentrations and vanishes abruptly down to 0 concentration exceeds 4M. The loss of current asymmetry through alpha-hemolysin is due to the denaturation of the channel's cap. We also show that the alpha-hemolysin pore inserted into a lipid bilayer is much more resistant to urea denaturation than the alpha-hemolysin monomer in solution: The pore remains in the lipid bilayer up to 7.2M urea. The pore formation is possible up to 4.66M urea when protein monomers were previously incubated in urea.