An inverted-type organic bulk-heterojunction solar cell inserting zinc oxide (ZnO) as an electron collection electrode, fluorine-doped tin oxide (FTO)/ZnO/[6,6]-phenyl-C(61)-butyric acid methyl ester:regioregular poly(3-hexylthiophene) (PCBM:P3HT)/poly(3,4-ethylenedioxylenethiophene):poly(4-styrenesulfonic acid) (PEDOT:PSS)/Au, was fabricated in air and characterized by an alternating current impedance spectroscopy (IS). In the IS measurement, we observed reproducibly the electric resistance and capacitance components originating from ZnO and organic active layers, and we found that the depletion layer functioning to take out the photocurrent to the external circuit was formed in both the ZnO and PCBM:P3HT layers at the ZnO/PCBM:P3HT interface. In this letter, we propose that this IS measurement is effective for evaluating the electric properties of several layers with capacitance components in organic thin-film solar cells.
An indium tin oxide/titanium oxide/[6,6]-phenyl C 61 butyric acid methyl ester: regioregular poly(3-hexylthiophene)/poly(3,4-ethylenedioxylenethiophene): poly(4-styrene sulfonic acid)/Au type organic solar cell (ITO/TiO x /PCBM:P3HT/PEDOT:PSS/Au) with 1 cm 2 active area, which is called "inverted type solar cell", was developed using an ITO/amorphous titanium oxide (TiO x ) electrode prepared by a sol-gel technique instead of the low functional electrode such as Al. The power conversion efficiency (η) of 2.47 % was obtained by irradiating AM 1.5G-100 mW cm -2 simulated sunlight. We found that a photoconduction of TiO x by irradiating UV light containing slightly into the simulated sunlight was required to drive this solar cell. The device durability in an ambient atmosphere was maintained for more than 20 h under continuous light irradiation. Further, when the air-stable device was covered by a glass plate with water getter sheet which was coated by an epoxy UV resin as sealing material, the durability was still higher and over 96 % of relative efficiency was observed even after continuous light irradiation for 120 h.
It is widely accepted that the conversion of the soluble, nontoxic amyloid β-protein (Aβ) monomer to aggregated toxic Aβ rich in β-sheet structures is central to the development of Alzheimer's disease. However, the mechanism of the abnormal aggregation of Aβ in vivo is not well understood. We have proposed that ganglioside clusters in lipid rafts mediate the formation of amyloid fibrils by Aβ, the toxicity and physicochemical properties of which are different from those of amyloids formed in solution. In this paper, the mechanism by which Aβ-(1-40) fibrillizes in raftlike lipid bilayers composed of monosialoganglioside GM1, cholesterol, and sphingomyelin was investigated in detail on the basis of singular-value decomposition of circular dichroism data and analysis of fibrillization kinetics. At lower protein densities in the membrane (Aβ:GM1 ratio of less than ∼0.013), only the helical species exists. At intermediate protein densities (Aβ:GM1 ratio between ∼0.013 and ∼0.044), the helical species and aggregated β-sheets (∼15-mer) coexist. However, the β-structure is stable and does not form larger aggregates. At Aβ:GM1 ratios above ∼0.044, the β-structure is converted to a second, seed-prone β-structure. The seed recruits monomers from the aqueous phase to form amyloid fibrils. These results will shed light on a molecular mechanism for the pathogenesis of the disease.
The conversion of the soluble, nontoxic amyloid-beta (Abeta) peptide into an aggregated, toxic form rich in beta-sheets is considered a key step in the development of Alzheimer's disease. Whereas growing evidence indicates that the Abeta amyloid fibrils consist of in-register parallel beta-sheets, little is known about the structure of soluble oligomeric intermediates because of their transient nature. To understand the mechanism by which amyloid fibrils form, especially the initial development of the "nucleus" oligomeric intermediates, we prepared covalently linked dimeric Abeta peptides and analyzed the kinetics of the fibril-forming process. A covalent bond introduced between two Abeta molecules dramatically facilitated the spontaneous formation of aggregates with a beta-sheet structure and affinity for thioflavin T. Transmission electron microscopy revealed, however, that these aggregates differed in morphology from amyloid fibrils, more closely resembling protofibrils. The protofibril-like aggregates were not the most thermodynamically stable state but were a kinetically trapped state. The results emphasize the importance of the conformational flexibility of the Abeta molecule and a balance in the association and dissociation rate for the formation of rigid amyloid fibrils.
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