Stretched-exponential a-Si:H/c-Si interface recombination decay

The electronic properties of hydrogenated amorphous silicon (a-Si:H) relax following stretched exponentials. This phenomenon was explained in the past by dispersive hydrogen diffusion, or by retrapping included hydrogen motion. In this letter, the authors report that the electronic passivation properties of intrinsic a-Si:H /crystalline silicon (c-Si) interfaces relax following a similar law. Carrier injection dependent a-Si:Hc-Si interface recombination calculations suggest this originates from amphoteric interface state (or Si dangling bond) reduction, rather than from a field effect. These findings underline the similarity between a-Si:Hc-Si interface recombination and the electronic properties of a-Si:H bulk material. © 2008 American Institute of Physics

Modification of textured silicon wafer surface morphology for fabrication of heterojunction solar cell with open circuit voltage over 700mV

Crystalline silicon wafer (c-Si) can be extremely well passivated by plasma enhanced chemical vapor deposited (PECVD) amorphous silicon (a-Si:H) films. As a result, on flat substrates, solar cells with very high open circuit voltage are readily obtained. On textured substrates however the passivation is more cumbersome, likely due to the presence of localized recombinative paths situated at the pyramid valleys. Here, we show that this issue may be resolved by selecting a silicon substrate morphology featuring large pyramids. Chemical post-texturization treatments can further reduce the surface recombination velocity. This sequence has allowed us to fabricate solar cells with open circuit voltage over 700 mV, demonstrating also on device level the effect of pyramid density and surface micro-roughness on the surface passivation quality

Properties of interfaces in amorphous/crystalline silicon heterojunctions

To study recombination at the amorphous/crystalline Si (a- Si:H/c-Si) heterointerface, the amphoteric nature of silicon (Si) dangling bonds is taken into account. Modeling interface recombination measured on various test structures provides insight into the microscopic passivation mechanisms, yielding an excellent interface defect density reduction by intrinsic a-Si:H and tunable field-effect passivation by doped layers. The potential of this model's applicability to recombination at other Si heterointerfaces is demonstrated. Solar cell properties of a-Si:H/c-Si heterojunctions are in good accordance with the microscopic interface properties revealed by modeling, that are, e.g., slight asymmetries in the neutral capture cross-sections and band offsets. The importance of atomically abrupt interfaces and the difficulties to obtain them on pyramidally textured c-Si is studied in combination with transmission electron microscopy

Optimization of KOH etching process to obtain textured substrates suitable for heterojunction solar cells fabricated by HWCVD

In this work, we have studied the texturization process of (100) c-Si wafers using a low concentration potassium hydroxide solution in order to obtain good quality textured wafers. The optimization of the etching conditions have led to random but uniform pyramidal structures with good optical properties. Then, symmetric heterojunctions were deposited by Hot-Wire CVD onto these substrates and the Quasi-Steady-State PhotoConductance technique was used to measure passivation quality. Little degradation in the effective lifetime and implicit open circuit voltage of these devices (< 20 mV) was observed in all cases. It is especially remarkable that for big uniform pyramids, the open-circuit voltage is comparable to the values obtained on flat substrates

Improved cardiovascular diagnostic accuracy by pocket size imaging device in non-cardiologic outpatients: the NaUSiCa (Naples Ultrasound Stethoscope in Cardiology) study

Miniaturization has evolved in the creation of a pocket-size imaging device which can be utilized as an ultrasound stethoscope. This study assessed the additional diagnostic power of pocket size device by both experts operators and trainees in comparison with physical examination and its appropriateness of use in comparison with standard echo machine in a non-cardiologic population

Alpha 2-adrenoceptors as a target for formamidine pesticides: in vitro and in vivo studies in mice

While the toxicity in insects of formamidines such as chlordimeform (CDM), its demethylated metabolite DCDM, and amitraz (AMZ) appears to involve activation of an octopamine-sensitive adenylate cyclase, their mechanism of action in mammals remains elusive. There is increasing evidence, however, that alpha 2-adrenoceptors might mediate certain effects of CDM, DCDM, and AMZ. In the present study, we investigated whether formamidines can interact directly with adrenoceptors in mouse forebrain both in vitro and after in vivo administration. Formamidines were potent inhibitors of the binding of [3H]clonidine to alpha 2-adrenoceptors with IC50's of 13 microM, 29 nM, and 130 nM for CDM, DCDM, and AMZ, respectively. Binding of [3H]yohimbine was inhibited with similar potencies. All compounds also inhibited with equal (CDM) or lower potency the binding of [3H]spiperone to dopamine D2 receptors and were weak inhibitors or inactive toward alpha 1- and beta-adrenoceptors, cholinergic muscarinic, GABAA, opiate mu, benzodiazepine, and histamine 1 receptors. Administration of formamidines to mice caused a dose-dependent decrease of [3H]clonidine binding. [3H]Clonidine binding returned to control values within 5 hr following administration of CDM and DCDM, but was still significantly decreased up to 48 hr after AMZ. Among different brain regions, [3H]clonidine binding was decreased to a larger extent in cerebral cortex, hippocampus, and midbrain. In vitro and ex vivo kinetic binding studies indicated that the effect of formamidines on alpha 2-adrenoceptors was due to a decrease in affinity and not to an alteration of the density of [3H]clonidine binding sites. The results of these biochemical studies support the hypothesis that alpha 2-adrenoceptors represent an important target for formamidine neurotoxicity in mammals

Acute and chronic effects of the pesticide amitraz on alpha 2-adrenoceptors in mouse brain

There is increasing evidence to suggest that several effects of the formamidine pesticide amitraz (AMZ) in mammals are mediated by its interaction with alpha 2-adrenoceptors. AMZ has been shown to inhibit the binding of [3H]clonidine, a specific ligand for alpha 2-adrenoceptors to mouse brain in vitro and after administration in vivo. In the present study we have further investigated and characterized the effects of acute and chronic administration of AMZ on brain alpha 2-adrenoceptors in mice. AMZ caused a dose-dependent inhibition of [3H]clonidine binding. This inhibition was long-lasting (more than 48 h) following a relatively high dose of AMZ (75 mg/kg), while it was of short duration (2 h) following low doses (7.5 and 12.5 mg/kg). The time course of inhibition of [3H]clonidine binding was correlated with the plasma levels of AMZ and/or its active metabolites, measured with a novel radioreceptor binding technique. The alteration of [3H]clonidine binding was due to a decrease in alpha 2-adrenoceptor affinity, with no change in the density of binding sites, and was reversible in vitro upon repeated washing of the membrane preparation. Repeated administration of 7.5 mg/kg or 12.5 mg/kg AMZ, to yield a total dose of 75 mg/kg, showed no evidence of a cumulative effect on brain alpha 2-adrenoceptors

Formamidine pesticides and alpha 2-adrenoceptors: studies with amitraz and chlordimeform in rats and development of a radioreceptor binding assay

The interaction of the formamidine pesticides chlordimeform (CDM) and amitraz (AMZ) with rat brain alpha2-adrenoceptors was investigated. Both compounds inhibited the binding of 3H-clonidine and 3H-yohimbine in vitro with IC50 values of 62-68 microM (CDM) and 95-110 nM (AMZ). In vivo administration of AMZ and CDM caused a dose-dependent inhibition of 3H-clonidine binding in rat forebrain. The inhibition was short-lasting (24 hr) following CDM administration, while after AMZ recovery of 3H-clonidine binding occurred only after 72 hr. Good correlations were found between inhibition of brain 3H-clonidine binding by the formamidines and "plasma equivalents" of these compounds and/or their biologically active metabolites, as measured by a new radioreceptor assay. These results suggest that 1) formamidines can interact in vivo with brain alpha 2-adrenoceptors when administered at doses previously shown to cause toxic effects on the central nervous system: and 2) this effect is reversible, both in vivo and in vitro, and appears to be linked to the presence of the formamidines and/or their active metabolites at the receptor sites

Acute and chronic effects of the pesticide amitraz on α2-adrenoceptors in the mouse brain

There is increasing evidence to suggest that several effects of the formamidine pesticide amitraz (AMZ) in mammals are mediated by its interaction with α2-adrenoceptors. AMZ has been shown to inhibit the binding of [3H]clonidine, a specific ligand for α2-adrenoceptors to mouse brain in vitro and after administration in vivo. In the present study we have further investigated and characterized the effects of acute and chronic administration of AMZ on brain α2-adrenoceptors in mice. AMZ caused a dosedependent inhibition of [3H]clonidine binding. This inhibition was long-lasting (more than 48 h) following a relatively high dose of AMZ (75 mg/kg), while it was of short duration (2 h) following low doses (7.5 and 12.5 mg/kg). The time course of inhibition of [3H]clonidine binding was correlated with the plasma levels of AMZ and/or its active metabolites, measured with a novel radioreceptor binding technique. The alteration of [3H]clonidine binding was due to a decrease in α2-adrenoceptor affinity, with no change in the density of binding sites, and was reversible in vitro upon repeated washing of the membrane preparation. Repeated administration of 7.5 mg/kg or 12.5 mg/kg AMZ, to yield a total dose of 75 mg/kg, showed no evidence of a cumulative effect on brain α2-adrenoceptors. © 1989