Pathway to the piezoelectronic transduction logic device.

The piezoelectronic transistor (PET) has been proposed as a transduction device not subject to the voltage limits of field-effect transistors. The PET transduces voltage to stress, activating a facile insulator-metal transition, thereby achieving multigigahertz switching speeds, as predicted by modeling, at lower power than the comparable generation field effect transistor (FET). Here, the fabrication and measurement of the first physical PET devices are reported, showing both on/off switching and cycling. The results demonstrate the realization of a stress-based transduction principle, representing the early steps on a developmental pathway to PET technology with potential to contribute to the IT industry.

Giant piezoresistive on/off ratios in rare-earth chalcogenide thin films enabling nanomechanical switching.

Sophisticated microelectromechanical systems for device and sensor applications have flourished in the past decade. These devices exploit piezoelectric, capacitive, and piezoresistive effects, and coupling between them. However, high-performance piezoresistivity (as defined by on/off ratio) has primarily been observed in macroscopic single crystals. In this Letter, we show for the first time that rare-earth monochalcogenides in thin film form can modulate a current by more than 1000 times due to a pressure-induced insulator to metal transition. Furthermore, films as thin as 8 nm show a piezoresistive response. The combination of high performance and scalability make these promising candidates for nanoscale applications, such as the recently proposed piezoelectronic transistor (PET). The PET would mechanically couple a piezoelectric thin film with a piezoresistive switching layer, potentially scaling to higher speeds and lower powers than today's complementary metal-oxide-semiconductor technology.

Room-temperature ferromagnetic nanotubes controlled by electron or hole doping.

Nanotubes and nanowires with both elemental (carbon or silicon) and multi-element compositions (such as compound semiconductors or oxides), and exhibiting electronic properties ranging from metallic to semiconducting, are being extensively investigated for use in device structures designed to control electron charge. However, another important degree of freedom--electron spin, the control of which underlies the operation of 'spintronic' devices--has been much less explored. This is probably due to the relative paucity of nanometre-scale ferromagnetic building blocks (in which electron spins are naturally aligned) from which spin-polarized electrons can be injected. Here we describe nanotubes of vanadium oxide (VO(x)), formed by controllable self-assembly, that are ferromagnetic at room temperature. The as-formed nanotubes are transformed from spin-frustrated semiconductors to ferromagnets by doping with either electrons or holes, potentially offering a route to spin control in nanotube-based heterostructures.

Two possible conducting states of the influenza A virus M2 ion channel.

Molecular dynamics simulations have been performed on protonated four-helix bundles based on the 25-residue Duff-Ashley transmembrane sequence of the M2 channel of the influenza A virus. Well-equilibrated tetrameric channels, with one, two and four of the H37 residues protonated, were investigated. The protonated peptide bundles were immersed in the octane portion of a phase-separated water/octane system, which provided a membrane-mimetic environment. The simulations suggest that there could be two conducting states of the M2 channel corresponding to tetramers containing one or two protonated histidines. The more open structure of the doubly protonated state suggests it would have the higher conductance.

The M2 channel of influenza A virus: a molecular dynamics study.

Molecular dynamics simulations have been performed on a tetramer of the 25-residue (SSDPLVVAASIIGILHLILWILDRL) synthetic peptide [1] which contains the transmembrane domain of the influenza A virus M2 coat protein. The peptide bundle was initially assembled as a parallel alpha-helix bundle in the octane portion of a phase separated water/octane system, which provided a membrane-mimetic environment. A 4-ns dynamics trajectory identified a left-handed coiled coil state of the neutral bundle, with a water filled funnel-like structural motif at the N-terminus involving the long hydrophobic sequence. The neck of the funnel begins at V27 and terminates at H37, which blocks the channel. The C-terminus is held together by inter-helix hydrogen bonds and contains water below H37. Solvation of the S23 and D24 residues, located at the rim of the funnel, appears to be important for stability of the structure. The calculated average tilt of the helices in the neutral bundle is 27 +/- 5 degrees, which agrees well with recent NMR data.

Molecular dynamics study of the LS3 voltage-gated ion channel.

Molecular dynamics calculations have been carried out on a model of the LS3 synthetic ion channel in a membrane mimetic environment. In the absence of an external electrostatic field, the LS3 channel, which consists of a bundle of six alpha-helices with sequence Ac-(LSSLLSL)3-CONH2, exhibits large structural fluctuations. However, in the presence of the field, the bundle adopts a well defined coiled-coil structure with an inner pore of water. The observed structural changes induced by the applied field are consistent with the proposed gating mechanism of the ion channel.

Molecular dynamics simulation of a synthetic ion channel.

A molecular dynamics simulation has been performed on a synthetic membrane-spanning ion channel, consisting of four alpha-helical peptides, each of which is composed of the amino acids leucine (L) and serine (S), with the sequence Ac-(LSLLLSL)3-CONH2. This four-helix bundle has been shown experimentally to act as a proton-conducting channel in a membrane environment. In the present simulation, the channel was initially assembled as a parallel bundle in the octane portion of a phase-separated water/octane system, which provided a membrane-mimetic environment. An explicit reversible multiple-time-step integrator was used to generate a dynamical trajectory, a few nanoseconds in duration for this composite system on a parallel computer, under ambient conditions. After more than 1 ns, the four helices were found to adopt an associated dimer state with twofold symmetry, which evolved into a coiled-coil tetrameric structure with a left-handed twist. In the coiled-coil state, the polar serine side chains interact to form a layered structure with the core of the bundle filled with H2O. The dipoles of these H2O molecules tended to align opposite the net dipole of the peptide bundle. The calculated dipole relaxation function of the pore H2O molecules exhibits two reorientation times. One is approximately 3.2 ps, and the other is approximately 100 times longer. The diffusion coefficient of the pore H2O is about one-third of the bulk H2O value. The total dipole moment and the inertia tensor of the peptide bundle have been calculated and reveal slow (300 ps) collective oscillatory motions. Our results, which are based on a simple united atom force-field model, suggest that the function of this synthetic ion channel is likely inextricably coupled to its dynamical behavior.

Molecular dynamics simulation of a hydrated diphytanol phosphatidylcholine lipid bilayer containing an alpha-helical bundle of four transmembrane domains of the influenza A virus M2 protein.

An alpha-helical bundle composed of four transmembrane portions of the M2 protein from the Influenza A virus has been studied in a hydrated diphytanol phosphatidylcholine bilayer using molecular dynamics (MD) calculations. Experimentally, the sequence utilized is known to aggregate as a four-helix bundle and act as a pH-gated proton-selective ion channel, which is blocked by the drug amantadine hydrochloride. In the presented simulation, the ion channel was initially set up as a parallel four-helix bundle. The all-atom simulation consisted of almost 16,000 atoms, described classically, using a forcefield from the CHARMM22 database. Bilayers with and without the bundle were shown to be stable throughout the nanosecond timescale of the MD simulation. Structural and dynamical properties of the bilayer both with and without the transmembrane protein are reported.