A novel single-chip 3-D multidimensional device for subsequent measurement of the three orthogonal magnetic-field components using one and the same transducer zone is presented. Six ohmic planar contacts on silicon substrate are implemented both as supply and four to obtain the full information about the vector components by three successive coupling arrangements realizing two in-plane sensitive and one orthogonal Hall effect devices. The proposed approach employs the same element, but at different time. The sensor operation is determined by the direction of individual parts of nonlinear carriers’ trajectory in the substrate and the Lorentz force action on them. The effective sensor resolution is 90x60x30 μm³. The respective channel- magnetosensitivities consists S_x ≈ 35 V/AT, S_y ≈ 26 V/AT, and S_z ≈ 18 V/AT, the channel cross-talk at induction B ≤ 1 T reaches no more than 3% and the lowest detected magnetic field of the three channels is about 10 μT in the frequency range f ≤ 10² Hz.

A novel functional multisensor for temperature and subsequent measurement of three orthogonal magnetic-field components using the same transducer zone is presented. One central emitter, two symmetrically positioned base contacts and two pairs of output ohmic terminals on a silicon substrate, close to the bases, are implemented. Three subsequent coupling arrangements of the output terminals use the same element at different times. Temperature is measured through the voltage on the forward biased p⁺-n emitter junction at constant supply current. The channel sensitivities are S_x = 7 V/AT, S_y = 9 V/AT and S_z = 11.3 V/AT. The thermo-sensitivity is K_EB = 1.82 mV/°C at supply current of 1 mA. Magnetic induction does not perturb thermometric voltage within a wide range, - 0.8 T ≤ B ≤ 0.8 T. The spatial resolution reaches about 110 х 90 х 40 μm³.

A 2D Hall microdevice for synchronous measurement of two in-plane magnetic-field components, using an original coupling concept based on two identical parallel-field three-contact (3C) silicon Hall elements positioned at right angle and integrated on the same chip, is presented. The two pairs of outer contacts of 3C Hall transducers are connected via two load resistors, converting simultaneously and independently the current changes in B_x and B_y magnetic fields into Hall voltages. Since the supply currents in both structures are equal, the magnetosensitivities are the same, too. At a fabrication of the devices on a common silicon chip, the output temperature drifts are perfectly matched. The high measurement accuracy, performance and compensated channel offsets of this 2D magnetometer are achieved by the minimal interface components between both sensors. The suggested sensing microsystem is appropriate for many contactless measurement instruments.

A new 2D (two-dimensional) in-plane sensitive Hall-effect sensor comprising two identical n-Si Greek-crosses is presented. Each of the crosses contains one central square contact and, symmetrically to each of their four sides, an outer contact is available. Outer electrode from one configuration is connected with the respective opposite contact from the other configuration, thus forming four parallel three-contact (3C) Hall elements. These original connections provide pairs of opposite supply currents in each of the cross-Hall structure. Also the obligatory load resistors in the outer contacts of 3С Hall elements are replaced by internal resistances of crosses themselves. The samples have been implemented by IC technology, using four masks. The magnetic field is parallel to the structures’ plane. The couples of opposite contacts of each Greek-cross are the outputs for the two orthogonal components of the magnetic vector at sensitivities S ≈ 115 V/AT whereas the cross-talk is very promising, reaching no more than 2.4%. The mean lowest detected magnetic induction B at a supply current I_s = 3 mA over the frequency range f ≤ 500 Hz at a signal to noise ratio equal to unity, is B_min ≈ 14 μT.

A novel coupling of two three-contact parallel-field Hall devices, ensuring almost full offset compensation and doubled output voltage at an increased signal-to-offset ratio is presented. The two silicon Hall elements are coupled as follows - the two pairs of outer contacts are connected via two load resistors of equal value converting simultaneously the current changes in a magnetic field into Hall voltage. Since the currents in both structures are opposite, the Hall voltages are equal in value but of opposite sign. At fabrication of the devices on the same silicon chip, the two offsets are almost equal and their temperature drifts are perfectly matched. The sensor output signal results from subtraction of two device output voltages using circuitry with three op-amps. The residual offset is about 150 times smaller than the internal ones. The obtained output voltage-to-residual offset ratio at channel magnetosensitivity of 76 V/AT is very promising, reaching 7x10³.

Many biomedical applications require a detailed understanding of the action of antimicrobial peptides on biological membranes. The cationic hemolytic peptide melittin, a major component of European honey bee (Apis mellifera) venom, is considered a model for elucidating lipid–protein interactions that are important for the function of biological systems. Here, we address the surface properties of human erythrocytes and rat liver mitochondrial membranes under in vitro melittin treatment. These membranes are negatively charged at neutral pH and represent primary targets of melittin’s effects in the onset of inflammatory diseases. The correlation between the functional activity of membrane systems and their surface electrical charge was assessed using microelectrophoresis, hemolysis assays, membrane transport measurements, lipid peroxidation analysis, and fluorescence microscopy. A mechanistic hypothesis for the divergent effects of sub-lytic, pre-pore doses of melittin on erythrocytes and mitochondria is discussed. At low concentrations, melittin interacts electrostatically with erythrocyte membranes, resulting in altered proton transport through the Band 3 protein. Melittin also induces changes in erythrocyte morphology and malondialdehyde content, as well as aggregation of mitochondrial vesicles. The electrokinetic mechanism of melittin action, associated with membrane stability, provides a novel perspective on its potential relevance to biomedical applications.