Discovery of intrinsic ferromagnetism in two-dimensional van der Waals crystals.

The realization of long-range ferromagnetic order in two-dimensional van der Waals crystals, combined with their rich electronic and optical properties, could lead to new magnetic, magnetoelectric and magneto-optic applications. In two-dimensional systems, the long-range magnetic order is strongly suppressed by thermal fluctuations, according to the Mermin-Wagner theorem; however, these thermal fluctuations can be counteracted by magnetic anisotropy. Previous efforts, based on defect and composition engineering, or the proximity effect, introduced magnetic responses only locally or extrinsically. Here we report intrinsic long-range ferromagnetic order in pristine Cr2Ge2Te6 atomic layers, as revealed by scanning magneto-optic Kerr microscopy. In this magnetically soft, two-dimensional van der Waals ferromagnet, we achieve unprecedented control of the transition temperature (between ferromagnetic and paramagnetic states) using very small fields (smaller than 0.3 tesla). This result is in contrast to the insensitivity of the transition temperature to magnetic fields in the three-dimensional regime. We found that the small applied field leads to an effective anisotropy that is much greater than the near-zero magnetocrystalline anisotropy, opening up a large spin-wave excitation gap. We explain the observed phenomenon using renormalized spin-wave theory and conclude that the unusual field dependence of the transition temperature is a hallmark of soft, two-dimensional ferromagnetic van der Waals crystals. Cr2Ge2Te6 is a nearly ideal two-dimensional Heisenberg ferromagnet and so will be useful for studying fundamental spin behaviours, opening the door to exploring new applications such as ultra-compact spintronics.

Alphaxalone Binds in Inner Transmembrane ß+-α- Interfaces of α1ß3γ2 γ-Aminobutyric Acid Type A Receptors.

BACKGROUND: Neurosteroids like alphaxalone are potent anxiolytics, anticonvulsants, amnestics, and sedative-hypnotics, with effects linked to enhancement of γ-aminobutyric acid type A (GABAA) receptor gating in the central nervous system. Data locating neurosteroid binding sites on synaptic αßγ GABAA receptors are sparse and inconsistent. Some evidence points to outer transmembrane ß-α interfacial pockets, near sites that bind the anesthetics etomidate and propofol. Other evidence suggests that steroids bind more intracellularly in ß-α interfaces. METHODS: The authors created 12 single-residue ß3 cysteine mutations: ß3T262C and ß3T266C in ß3-M2; and ß3M283C, ß3Y284C, ß3M286C, ß3G287C, ß3F289C, ß3V290C, ß3F293C, ß3L297C, ß3E298C, and ß3F301C in ß3-M3 helices. The authors coexpressed α1 and γ2L with each mutant ß3 subunit in Xenopus oocytes and electrophysiologically tested each mutant for covalent sulfhydryl modification by the water-soluble reagent para-chloromercuribenzenesulfonate. Then, the authors assessed whether receptor-bound alphaxalone, etomidate, or propofol blocked cysteine modification, implying steric hindrance. RESULTS: Eleven mutant ß3 subunits, when coexpressed with α1 and γ2L, formed functional channels that displayed varied sensitivities to the three anesthetics. Exposure to para-chloromercuribenzenesulfonate produced irreversible functional changes in ten mutant receptors. Protection by alphaxalone was observed in receptors with ß3V290C, ß3F293C, ß3L297C, or ß3F301C mutations. Both etomidate and propofol protected receptors with ß3M286C or ß3V290C mutations. Etomidate also protected ß3F289C. In α1ß3γ2L structural homology models, all these protected residues are located in transmembrane ß-α interfaces. CONCLUSIONS: Alphaxalone binds in transmembrane ß-α pockets of synaptic GABAA receptors that are adjacent and intracellular to sites for the potent anesthetics etomidate and propofol.

Radio Frequency Tunable Oscillator Device Based on a SmB_{6} Microcrystal.

Radio frequency tunable oscillators are vital electronic components for signal generation, characterization, and processing. They are often constructed with a resonant circuit and a "negative" resistor, such as a Gunn diode, involving complex structure and large footprints. Here we report that a piece of SmB_{6}, 100 µm in size, works as a current-controlled oscillator in the 30 MHz frequency range. SmB_{6} is a strongly correlated Kondo insulator that was recently found to have a robust surface state likely to be protected by the topology of its electronics structure. We exploit its nonlinear dynamics, and demonstrate large ac voltage outputs with frequencies from 20 Hz to 30 MHz by adjusting a small dc bias current. The behaviors of these oscillators agree well with a theoretical model describing the thermal and electronic dynamics of coupled surface and bulk states. With reduced crystal size we anticipate the device to work at higher frequencies, even in the THz regime. This type of oscillator might be realized in other materials with a metallic surface and a semiconducting bulk.

A Cysteine Substitution Probes ß3H267 Interactions with Propofol and Other Potent Anesthetics in α1ß3γ2L γ-Aminobutyric Acid Type A Receptors.

BACKGROUND: Anesthetic contact residues in γ-aminobutyric acid type A (GABAA) receptors have been identified using photolabels, including two propofol derivatives. O-propofol diazirine labels H267 in ß3 and α1ß3 receptors, whereas m-azi-propofol labels other residues in intersubunit clefts of α1ß3. Neither label has been studied in αßγ receptors, the most common isoform in mammalian brain. In αßγ receptors, other anesthetic derivatives photolabel m-azi-propofol-labeled residues, but not ßH267. The authors' structural homology model of α1ß3γ2L receptors suggests that ß3H267 may abut some of these sites. METHODS: Substituted cysteine modification-protection was used to test ß3H267C interactions with four potent anesthetics: propofol, etomidate, alphaxalone, and R-5-allyl-1-methyl-5-(m-trifluoromethyl-diazirinylphenyl) barbituric acid (mTFD-MPAB). The authors expressed α1ß3γ2L or α1ß3H267Cγ2L GABAA receptors in Xenopus oocytes. The authors used voltage clamp electrophysiology to assess receptor sensitivity to γ-aminobutyric acid (GABA) and anesthetics and to compare p-chloromercuribenzenesulfonate modification rates with GABA versus GABA plus anesthetics. RESULTS: Enhancement of low GABA (eliciting 5% of maximum) responses by equihypnotic concentrations of all four anesthetics was similar in α1ß3γ2L and α1ß3H267Cγ2L receptors (n > 3). Direct activation of α1ß3H267Cγ2L receptors, but not α1ß3γ2L, by mTFD-MPAB and propofol was significantly greater than the other anesthetics. Modification of ß3H267C by p-chloromercuribenzenesulfonate (n > 4) was rapid and accelerated by GABA. Only mTFD-MPAB slowed ß3H267C modification (approximately twofold; P = 0.011). CONCLUSIONS: ß3H267 in α1ß3γ2L GABAA receptors contacts mTFD-MPAB, but not propofol. The study results suggest that ß3H267 is near the periphery of one or both transmembrane intersubunit (α+/ß- and γ+/ß-) pockets where both mTFD-MPAB and propofol bind.

Tryptophan and Cysteine Mutations in M1 Helices of α1ß3γ2L γ-Aminobutyric Acid Type A Receptors Indicate Distinct Intersubunit Sites for Four Intravenous Anesthetics and One Orphan Site.

BACKGROUND: γ-Aminobutyric acid type A (GABAA) receptors mediate important effects of intravenous general anesthetics. Photolabel derivatives of etomidate, propofol, barbiturates, and a neurosteroid get incorporated in GABAA receptor transmembrane helices M1 and M3 adjacent to intersubunit pockets. However, photolabels have not been consistently targeted at heteromeric αßγ receptors and do not form adducts with all contact residues. Complementary approaches may further define anesthetic sites in typical GABAA receptors. METHODS: Two mutation-based strategies, substituted tryptophan sensitivity and substituted cysteine modification-protection, combined with voltage-clamp electrophysiology in Xenopus oocytes, were used to evaluate interactions between four intravenous anesthetics and six amino acids in M1 helices of α1, ß3, and γ2L GABAA receptor subunits: two photolabeled residues, α1M236 and ß3M227, and their homologs. RESULTS: Tryptophan substitutions at α1M236 and positional homologs ß3L231 and γ2L246 all caused spontaneous channel gating and reduced γ-aminobutyric acid EC50. Substituted cysteine modification experiments indicated etomidate protection at α1L232C and α1M236C, R-5-allyl-1-methyl-5-(m-trifluoromethyl-diazirinylphenyl) barbituric acid protection at ß3M227C and ß3L231C, and propofol protection at α1M236C and ß3M227C. No alphaxalone protection was evident at the residues the authors explored, and none of the tested anesthetics protected γ2I242C or γ2L246C. CONCLUSIONS: All five intersubunit transmembrane pockets of GABAA receptors display similar allosteric linkage to ion channel gating. Substituted cysteine modification and protection results were fully concordant with anesthetic photolabeling at α1M236 and ß3M227 and revealed overlapping noncongruent sites for etomidate and propofol in ß-α interfaces and R-5-allyl-1-methyl-5-(m-trifluoromethyl-diazirinylphenyl) barbituric acid and propofol in α-ß and γ-ß interfaces. The authors' results identify the α-γ transmembrane interface as a potentially unique orphan modulator site.

Observation of Quantum Anomalous Hall Effect and Exchange Interaction in Topological Insulator/Antiferromagnet Heterostructure.

Integration of a quantum anomalous Hall insulator with a magnetically ordered material provides an additional degree of freedom through which the resulting exotic quantum states can be controlled. Here, an experimental observation is reported of the quantum anomalous Hall effect in a magnetically-doped topological insulator grown on the antiferromagnetic insulator Cr2 O3 . The exchange coupling between the two materials is investigated using field-cooling-dependent magnetometry and polarized neutron reflectometry. Both techniques reveal strong interfacial interaction between the antiferromagnetic order of the Cr2 O3 and the magnetic topological insulator, manifested as an exchange bias when the sample is field-cooled under an out-of-plane magnetic field, and an exchange spring-like magnetic depth profile when the system is magnetized within the film plane. These results identify antiferromagnetic insulators as suitable candidates for the manipulation of magnetic and topological order in topological insulator films.

Discovery of a magnetic conductive interface in PbZr0.2Ti0.8O3 /SrTiO3 heterostructures.

Emergent physical properties often arise at interfaces of complex oxide heterostructures due to the interplay between various degrees of freedom, especially those with polar discontinuities. It is desirable to explore if these structures may generate pure and controllable spin currents, which are needed to attain unmatched performance and energy efficiency in the next-generation spintronic devices. Here we report the emergence of a spin-polarized two-dimensional electron gas (SP-2DEG) at the interface of two insulators, SrTiO3 and PbZr0.2Ti0.8O3. This SP-2DEG is strongly localized at the interfacial Ti atoms, due to the interplay between Coulomb interaction and band bending, and can be tuned by the ferroelectric polarization. Our findings open a door for engineering ferroelectric/insulator interfaces to create tunable ferroic orders for magnetoelectric device applications and provide opportunities for designing multiferroic materials in heterostructures.

Time-reversal symmetry-breaking superconductivity in epitaxial bismuth/nickel bilayers.

Superconductivity that spontaneously breaks time-reversal symmetry (TRS) has been found, so far, only in a handful of three-dimensional (3D) crystals with bulk inversion symmetry. We report an observation of spontaneous TRS breaking in a 2D superconducting system without inversion symmetry: the epitaxial bilayer films of bismuth and nickel. The evidence comes from the onset of the polar Kerr effect at the superconducting transition in the absence of an external magnetic field, detected by the ultrasensitive loop-less fiber-optic Sagnac interferometer. Because of strong spin-orbit interaction and lack of inversion symmetry in a Bi/Ni bilayer, superconducting pairing cannot be classified as singlet or triplet. We propose a theoretical model where magnetic fluctuations in Ni induce the superconducting pairing of the [Formula: see text] orbital symmetry between the electrons in Bi. In this model, the order parameter spontaneously breaks the TRS and has a nonzero phase winding number around the Fermi surface, thus making it a rare example of a 2D topological superconductor.

Mutations at beta N265 in γ-aminobutyric acid type A receptors alter both binding affinity and efficacy of potent anesthetics.

Etomidate and propofol are potent general anesthetics that act via GABAA receptor allosteric co-agonist sites located at transmembrane ß+/α- inter-subunit interfaces. Early experiments in heteromeric receptors identified ßN265 (M2-15') on ß2 and ß3 subunits as an important determinant of sensitivity to these drugs. Mechanistic analyses suggest that substitution with serine, the ß1 residue at this position, primarily reduces etomidate efficacy, while mutation to methionine eliminates etomidate sensitivity and might prevent drug binding. However, the ßN265 residue has not been photolabeled with analogs of either etomidate or propofol. Furthermore, substituted cysteine modification studies find no propofol protection at this locus, while etomidate protection has not been tested. Thus, evidence of contact between ßN265 and potent anesthetics is lacking and it remains uncertain how mutations alter drug sensitivity. In the current study, we first applied heterologous α1ß2N265Cγ2L receptor expression in Xenopus oocytes, thiol-specific aqueous probe modification, and voltage-clamp electrophysiology to test whether etomidate inhibits probe reactions at the ß-265 sidechain. Using up to 300 µM etomidate, we found both an absence of etomidate effects on α1ß2N265Cγ2L receptor activity and no inhibition of thiol modification. To gain further insight into anesthetic insensitive ßN265M mutants, we applied indirect structure-function strategies, exploiting second mutations in α1ß2/3γ2L GABAA receptors. Using α1M236C as a modifiable and anesthetic-protectable site occupancy reporter in ß+/α- interfaces, we found that ßN265M reduced apparent anesthetic affinity for receptors in both resting and GABA-activated states. ßN265M also impaired the transduction of gating effects associated with α1M236W, a mutation that mimics ß+/α- anesthetic site occupancy. Our results show that ßN265M mutations dramatically reduce the efficacy/transduction of anesthetics bound in ß+/α- sites, and also significantly reduce anesthetic affinity for resting state receptors. These findings are consistent with a role for ßN265 in anesthetic binding within the ß+/α- transmembrane sites.