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The catalytic performance of metal nanoparticles (NPs), including activity, selectivity, and durability, depends on their shape and structure at the molecular level. Consequently, metal NPs of different size and shape, e.g., nanobelts, nanocubes, nanoflakes, and nanowires, demonstrate different reactivity and provide different reaction rates depending on the facet exposed. In this context, the present review aims to summarize the shape-structure–activity relation of metallic nanocatalysts. Moreover, keeping in mind that the application of noble metal catalysts is expensive, we would like to draw the reader's attention to bimetallic nanocatalysts supported on graphitic carbon nitride. One of the advantages of these systems is the possibility to minimize the use of noble metals by introducing another metal either to the parent NPs and/or modifying the support materials. The development and optimization of bimetallic nanocatalysts might provide the new class of materials with superior, tunable performance, thermal stability and reduced costs compared to presently available commercial catalysts. Therefore, further application of these bimetallic composites for sustainable development in energy, green chemicals/fuels and environmental protection will be discussed.

The electrochemical impedance spectroscopy (EIS) and polarization-modulation infrared reflection absorption spectroscopy (PM-IRRAS) techniques were employed to study the ionophore properties of valinomycin in a model floating bilayer lipid membrane (fBLM) in perchlorate supporting electrolytes with potassium and sodium cations. Valinomycin decreases the membrane resistance of the fBLM in KClO4 solution by about 180 times, while it has a negligible effect on the membrane resistivity in NaClO4 solution. The IR spectra indicate that valinomycin forms a complex with K+, but not with Na+. The valinomycin-K+ complex adopts a small tilt angle with respect to the electrode surface normal and is well interdigitated between the acyl chains of the bilayer. The EIS and PM-IRRAS results indicate that valinomycin forms complexes with K+ and transports K+ across the lipid bilayer. This transport is potential independent and hence has a passive character.

Neurodegeneration in Alzheimer's disease is associated with disruption of the neuronal cell membrane by the amyloid β (Aβ) peptide. However, the disruption mechanism and the resulting changes in membrane properties remain to be elucidated. To address this issue, herein the interaction of amyloid β monomers (AβMs) and amyloid β oligomers (AβOs) with a floating bilayer lipid membrane (fBLM) was studied using electrochemical and IR spectroscopy techniques. IR measurements showed that both Aβ forms interacted similarly with the hydrophobic membrane core (lipid acyl chains), causing conformational and orientational changes of the lipid acyl chains, thus decreasing acyl chain mobility and altering the lipid packing unit cell. In the presence of AβOs, these changes were more significant than those in the presence of AβMs. However, respective interactions of AβMs and AβOs with the membrane hydrophilic exterior (lipid heads) were quite different. AβMs dehydrated lipid heads without affecting their orientation while AβOs changed the orientation of lipid heads keeping their hydration level intact. Electrochemical measurements showed that only AβOs porated the fBLM, thus significantly changing the fBLM electrical properties. The present results provide new molecular-level insight into the mechanism of membrane destruction by AβOs and changes in the membrane properties.

Protein misfolding diseases, like Alzheimer's, Parkinson's, and Huntington's disease, are associated with misfolded protein aggregation. Alzheimer's disease is related to a progressive neuronal death induced by small amyloid β oligomers. Here, we describe the procedure to prepare and identify different types of small toxic amyloid β oligomers by atomic force microscopy (AFM).

Protein misfolding diseases, like Alzheimer's, Parkinson's, and Huntington's disease, are associated with misfolded protein aggregation. Alzheimer's disease is related to a progressive neuronal death induced by small amyloid β oligomers. Here, we describe the procedure to prepare and identify different types of small toxic amyloid β oligomers by atomic force microscopy (AFM).

Within the Waste2Fuel project, innovative, high-performance, and cost-effective fuel production methods are developed to target the “closed carbon cycle”. The catalysts supported on different metal oxides were characterized by XRD, XPS, Raman, UV-Vis, temperature-programmed techniques, then, they were tested in CO2 hydrogenation at 1 bar. Moreover, the V2O5 promotion was studied for Ni/Al2O3 catalyst. The precisely designed hydrotalcite-derived catalyst and vanadia-promoted Ni-catalysts deliver exceptional conversions for the studied processes, presenting high durability and selectivity, outperforming the best-known catalysts. The equilibrium conversion was reached at temperatures around 623 K, with the primary product of reaction CH4 (&gt, 97% CH4 yield). Although the Ni loading in hydrotalcite-derived NiWP is lower by more than 40%, compared to reference NiR catalyst and available commercial samples, the activity increases for this sample, reaching almost equilibrium values (GHSV = 1.2 × 104 h–1, 1 atm, and 293 K).

Single‐atom catalysts (SACs) are highly enviable to exploit the utmost utilization of metallic catalysts; their efficiency by utilizing nearly all atoms to often exhibit high catalytic performances. To architect the isolated single atom on an ideal solid support with strong coordination has remained a crucial trial. Herein, graphene functionalized with nitrile groups (cyanographene) as an ideal support to immobilize isolated copper atoms G(CN)‐Cu with strong coordination is reported. The precisely designed mixed‐valence single atom copper (G(CN)‐Cu) catalysts deliver exceptional conversions for electrochemical methanol oxidation (MOR) and CO2reduction (CO2RR) targeting a “closed carbon cycle.” An onset of MOR and CO2RR are obtained to be ≈0.4V and ≈−0.7 versus Ag/AgCl, respectively, with single active sites located in an unsaturated coordination environment, it being the most active Cu sites for both studied reactions. Moreover, G(CN)‐Cu exhibited significantly lower resistivity and higher current density toward MOR and CO2RR than observed for reference catalysts.

Alzheimer's disease (AD) is characterized by progressive neurodegeneration associated with amyloid β (Aβ) peptide aggregation. The aggregation of Aβ monomers (AβMs) leads to the formation of Aβ oligomers (AβOs), the neurotoxic Aβ form, capable of permeating the cell membrane. Here, we investigated the effect of a fluorene-based active drug candidate, named K162, on both Aβ aggregation and AβO toxicity toward the bilayer lipid membrane (BLM). Electrochemical impedance spectroscopy (EIS), atomic force microscopy (AFM), and molecular dynamics (MD) were employed to show that K162 inhibits AβOs-induced BLM permeation, thus preserving BLM integrity. In the presence of K162, only shallow defects on the BLM surface were formed. Apparently, K162 modifies Aβ aggregation by bypassing the formation of toxic AβOs, and only nontoxic AβMs, dimers (AβDs), and fibrils (AβFs) are produced. Unlike other Aβ toxicity inhibitors, K162 preserves neurologically beneficial AβMs. This unique K162 inhibition mechanism provides an alternative AD therapeutic strategy that could be explored in the future.

Correction for ‘Bimetallic nanocatalysts supported on graphitic carbon nitride for sustainable energy development: the shape-structure–activity relation’ by Ewelina Kuna et al., Nanoscale Adv., 2021, 3, 1342–1351, DOI: 10.1039/D0NA01063D.

Topography and nanomechanical properties of the supported 1,2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC) single bilayer in the ripple phase were investigated by atomic force microscopy with the use of PeakForce Quantitative Nanomechanical Mapping (PF-QNM) mode under liquid conditions. The DMPC single bilayer was deposited on the mica surface by Langmuir-Blodgett and Langmuir-Schaefer techniques combined. Next, the sample was stored overnight at 4 °C under buffer solution (pH = 7.6) in the presence of tris(hydroxymethyl)aminomethane, (Tris), and then, AFM imaging was performed at 21 °C using the same buffer. The AFM topography images revealed the presence of a periodic structure with an average wavelength of 96.0 ± 7.8 nm and an average amplitude of 0.97 ± 0.03 nm. This macro-ripple structure was asymmetric and formed by long ripples composed of two stripes of different heights. The changes in topography were accompanied by local changes in the Young's modulus, which indicate that the nanomechanical properties of the bilayer are not evenly distributed, namely, the higher stripes are characterized by a lower Young's modulus than that calculated for lower stripes of the ripples. This indicates that the ripple phase is composed of phospholipid molecules of periodically changed orientation and conformation characteristic for fluid-like and gel-like state of DMPC.

Amyloid β, Aβ(1-42), is a component of senile plaques present in the brain of Alzheimer's disease patients and one of the main suspects responsible for pathological consequences of the disease. Herein, we directly visualize the Aβ activity toward a brain-like model membrane and demonstrate that this activity strongly depends on the Aβ oligomer size. PeakForce quantitative nanomechanical mapping mode of atomic force microscopy imaging revealed that the interaction of large-size (LS) Aβ oligomers, corresponding to high-molecular-weight Aβ oligomers, with the brain total lipid extract (BTLE) membrane resulted in accelerated Aβ fibrillogenesis on the membrane surface. Importantly, the fibrillogenesis did not affect integrity of the membrane. In contrast, small-size (SS) Aβ oligomers, corresponding to low-molecular-weight Aβ oligomers, created pores and then disintegrated the BTLE membrane. Both forms of the Aβ oligomers changed nanomechanical properties of the membrane by decreasing its Young's modulus by ∼45%. Our results demonstrated that both forms of Aβ oligomers induce the neurotoxic effect on the brain cells but their action toward the membrane differs significantly.

Disruption of the neuronal membrane by toxic amyloid β oligomers is hypothesized to be the major event associated with Alzheimer's disease's neurotoxicity. Misfolding of amyloid β is followed by aggregation via different pathways in which structurally different amyloid β oligomers can be formed. The respective toxic actions of these structurally diverse oligomers can vary significantly. Linking a particular toxic action to a structurally unique kind of amyloid β oligomers and resolving their toxicity-determining feature remains challenging because of their transient stability and heterogeneity. Moreover, the lipids that make up the membrane affect amyloid β oligomers' behavior, thus adding to the problem's complexity. The present review compares and analyzes the latest results to improve understanding of amyloid β oligomers' interaction with lipid bilayers.