We introduce new hole-selective contacts for next-generation perovskite photovoltaics and point to design paths for molecular engineering of perfect interfaces.

Comparison of conventional and newly developed laccase-based electrocatalytic systems for oxygen reduction.

Water is required for biological function of tethered bilayer lipid membranes (tBLMs) consisting of a lipid bilayer anchored by a mixed self-assembled monolayer (SAM) to a solid support. In this work, water-induced structural changes in mixed SAMs and bonding with gold substrate were probed in situ by the isotope-edited SERS coupled with the first-principles calculations. The assignment of the bands was based on experimental analysis of deuterated 2-mercaptoethanol (ME-D 4 ) and quantum chemical modeling of adsorption complexes consisting of a Au cluster of 10 atoms. Evidence for interaction of the gauche conformer with the Au surface through both S and O atoms was obtained from the analysis of the Au−S/Au−O vibrational mode near 303 cm −1 and adsorptioninduced downshift of the C−O stretching band near 1100 cm −1 . First-principles calculations of adsorption complexes revealed shortening of the Au−O bond upon hydrogen bonding of explicit water molecule to the OH group of ME-D 4 . Intense bands in the SERS spectrum near 679 and 597 cm −1 were assigned to C−S vibrational modes of adsorbed ME-D 4 in trans and gauche conformation, respectively. Analysis of relative intensities revealed a decrease in relative amount of trans conformers after 72 h incubation of the SAM in water. At the same time an increase in the population of a long carbon chain molecular anchor (WC14) in the all-trans hydrocarbon chain conformation was detected by SERS. Observed structural changes suggest water-induced clustering of long-chain anchors and conformational transition for short-chain thiols.

Encapsulation of proteins within lipid inverse bicontinuous cubic phases (Q 2 ) has been widely studied for many applications, such as protein crystallization or drug delivery of proteins for food and pharmaceutical purposes. However, the use of the lipid sponge (L 3 ) phase for encapsulation of proteins has not yet been well explored. Here, we have employed a lipid system that forms highly swollen sponge phases to entrap aspartic protease (34 kDa), an enzyme used for food processing, e.g., to control the cheese-ripening process. Small-angle x-ray scattering showed that although the L 3 phase was maintained at low enzyme concentrations (%15 mg/mL), higher concentration induces a transition to more curved structures, i.e., transition from L 3 to inverse bicontinuous cubic (Q 2 ) phase. The Raman spectroscopy data showed minor conformational changes assigned to the lipid molecules that confirm the lipid-protein interactions. However, the peaks assigned to the protein showed that the structure was not significantly affected. This was consistent with the higher activity presented by the encapsulated aspartic protease compared to the free enzyme stored at the same temperature. Finally, the encapsulation efficiency of aspartic protease in lipid sponge-like nanoparticles was 81% as examined by size-exclusion chromatography. Based on these results, we discuss the large potential of lipid sponge phases as carriers for proteins.

Effects of amyloid beta (Aβ) oligomers on viability and function of cell lines such as NB4 (human acute promyelocytic leukemia), A549 (human lung cancer (adenocarcinomic alveolar basal epithelial tumor)) and MCF-7 (human breast cancer (invasive breast ductal carcinoma)) were investigated. Two types of Aβ oligomers were used in the study. The first type was produced in the presence of oligomerization inhibitor, hexafluoroisopropanol (HFIP). The second type of amyloids was assembled in the absence of the inhibitor. The first type preparation was predominantly populated with dimers and trimers, while the second type contained mostly pentadecamers. These amyloid species exhibited different secondary protein structure with considerable amount of antiparallel β sheet structural elements in HFIP oligomerized Aβ mixtures. The effect of the cell growth inhibition, which was stronger in the case of HFIP Aβ oligomers, was observed for all cell lines. Tests aiming at elucidating the effects of the amyloid species on cell cycles showed little differences between amyloid preparations. This prompts us to conclude that the effect on the cancer cell proliferation rate is less specific to the biological processes developing inside the cells during the proliferation. Therefore, cell growth inhibition may involve interactions with the peripheral parts of the cancer cells, such as a phospholipid membrane, and only in case of the NB4 cells, where accumulation of amyloid species inside the cells was detected, one may imply the opposite. In general, cancer cells were much less susceptible to the damaging effects of amyloid oligomers compared to earlier observations in mixed neuronal cell cultures.