A computational platform for the virtual unfolding of Herculaneum Papyri.

Ancient Herculaneum papyrus scrolls, hopelessly charred in the 79 A.D. Vesuvius eruption, contain valuable writings of the Greek philosophers of the day, including works of the Epicurean Philodemus. X-ray phase contrast tomography has recently begun unlocking their secrets. However, only small portions of the text hidden inside the scroll have been recover. One of the challenging tasks in Herculaneum papyri investigation is their virtual unfolding because of their highly complicated structure and three-dimensional arrangement. Although this procedure is feasible, problems in segmentation and flattening hinder the unrolling of a large portion of papyrus. We propose a computational platform for the virtual unfolding procedure, and we show the results of its application on two Herculaneum papyrus fragments. This work paves the way to a comprehensive survey and to further interpretation of larger portions of text hidden inside the carbonized Herculaneum papyri.

Zinc(II) tetraphenylporphyrin on Au(111) investigated by scanning tunnelling microscopy and photoemission spectroscopy measurements.

Porphyrins are a versatile class of molecules, which have attracted attention over the years due to their electronic, optical and biological properties. Self-assembled monolayers of porphyrins were widely studied on metal surfaces in order to understand the supramolecular organization of these molecules, which is a crucial step towards the development of devices starting from the bottom-up approach. This perspective could lead to tailor the interfacial properties of the surface, depending on the specific interaction between the molecular assembly and the metal surface. In this study, we revisit the investigation of the assembly of zinc-tetraphenylporphyrins on Au(111) in order to explore the adsorption of the molecular network on the noble metal substrate. The combined analysis of scanning tunneling microscopy (STM) imaging and core levels photoemission spectroscopy measurements support a peculiar arrangement of the ZnTPP molecular network, with Zn atoms occupying the bridge sites of the Au surface atoms. Furthermore, we prove that, at few-layers coverage, the interaction between the deposited layers allows a relevant molecular mobility of the adlayer, as observed by STM and supported by core levels photoemission analysis.

Adsorption of Nile Red Self-Assembled Monolayers on Au(111).

The ability of Nile Red to self-assemble into supramolecular packings on Au(111) was studied using scanning tunneling microscopy and modeled through theoretical semiempirical calculations. At both submonolayer (sub-ML) and ML coverages, two distinct molecular packings, that is, four-leaf clover and dense chain, were observed, both weakly interacting with the underlying metal surface. Theoretical calculations suggested that the dipole moment plays a subtle role in both molecular assemblies, held together by hydrogen bonds between the Nile Red molecules. Furthermore, although both molecular assemblies were observed in as-deposited samples, a mild thermal annealing caused the transition from the four-leaf clover to the dense-chain packing, pointing out the greater stability of the dense-chain configuration. The study further emphasized how the established interactions between the Nile Red molecules are strongly influenced by the surrounding environment.

Gi Protein Modulation of the Potassium Channel TASK-2 Mediates Vesicle Osmotic Swelling to Facilitate the Fusion of Aquaporin-2 Water Channel Containing Vesicles.

Vesicle fusion is a fundamental cell biological process similar from yeasts to humans. For secretory vesicles, swelling is considered a step required for the expulsion of intravesicular content. Here this concept is revisited providing evidence that it may instead represent a general mechanism. We report the first example that non-secretory vesicles, committed to insert the Aquaporin-2 water channel into the plasma membrane, swell and this phenomenon is required for fusion to plasma membrane. Through an interdisciplinary approach, using atomic force microscope (AFM), a fluorescence-based assay of vesicle volume changes and NMR spectroscopy to measure water self-diffusion coefficient, we provide evidence that Gi protein modulation of potassium channel TASK-2 localized in AQP2 vesicles, is required for vesicle swelling. Estimated intravesicular K⁺ concentration in AQP2 vesicles, as measured by inductively coupled plasma mass spectrometry, was 5.3 mM, demonstrating the existence of an inwardly K⁺ chemical gradient likely generating an osmotic gradient causing vesicle swelling upon TASK-2 gating. Of note, abrogation of K⁺ gradient significantly impaired fusion between vesicles and plasma membrane. We conclude that vesicle swelling is a potentially important prerequisite for vesicle fusion to the plasma membrane and may be required also for other non-secretory vesicles, depicting a general mechanism for vesicle fusion.

Evidence of confinement of the π plasmon in periodically rippled graphene on Ru(0001).

High-resolution electron energy loss spectroscopy has been used to study the electronic response of periodically rippled monolayer graphene grown on Ru(0001). A plasmonic mode, assigned to the π plasmon, has been observed at around 6 eV. The dispersion curve of this collective mode indicates plasmon confinement within the hills of the ripples. Moreover, we found that the corrugation of the graphene sheet also significantly affects the damping processes of the π plasmon.

Short-range interactions in Na coadsorption with CO and O on Ni(111).

The coadsorption of Na with CO and O on Ni(111) is studied by high-resolution electron energy loss spectroscopy. Experimental evidence for a very short-range interaction between Na and coadsorbates is reported, in contrast with recent theoretical predictions overestimating nonlocal alkali-induced effects. Loss spectra show distinct features, as a consequence of different local [CO]:[Na] and [O]:[Na] stoichiometries.

Hypotonicity induces aquaporin-2 internalization and cytosol-to-membrane translocation of ICln in renal cells.

Kidney collecting-duct cells swell in response to changes in medulla osmolality caused by the transition from antidiuresis to diuresis. Regulatory volume decrease (RVD) mechanisms must be activated to face this hypotonic stress. In Aquaporin-2 (AQP2)-expressing renal CD8 cells, hypotonicity decreased cell surface expression of AQP2 and increased the amount of AQP2 localized intracellularly, whereas the total amount of AQP2 phosphorylated at ser-256 decreased. Analysis of cAMP dynamics using fluorescence resonance energy transfer (FRET) showed that hypotonicity causes a reduction of cAMP, consistent with a decrease in phospho-AQP2. Moreover, hypotonicity caused a profound actin reorganization, associated with the loss of stress fibers and formation of F-actin patches (microspikes) at the cell border. Those changes were regulated by the monomeric GTPase Cdc42. Interestingly, expression of the dominant-negative Cdc42 (N17-Cdc42) prevented the hypotonicity-induced microspike formation and the generation of Cl(-) currents. Hypotonicity also caused the relocation from the cytosol to the plasma membrane and increase in interaction with actin of ICln (nucleotide-sensitive chloride current protein), which is essential for the generation of ion currents activated during RVD. Together, the profound actin remodeling, internalization of AQP2 and translocation of ICln to the plasma membrane during hypotonicity may contribute to RVD after cell swelling in renal medulla.