Search

In this work, a system consisting of two resistive sensors working in tandem to detect and quantify the acetic acid released during the degradation of cellulose acetate-based ancient cinematographic and photographic films is presented. Acetic acid must be constantly monitored to prevent reaching concentrations at which autocatalytic degradation processes begin. The sensors are constituted by a thin layer of metal oxide (tungsten oxide and tin oxide) deposited over an interdigitated electrode capable of being heated, chosen to maximize the array response towards acetic acid vapors. The signals obtained from the sensor array are mathematically processed to reduce the background signal due to interferent gases produced during degradation of ancient cinematographic films. The sensor array reported a LOD of 30 ppb for acetic acid, with a linearity range up to 30 ppm. Finally, the sensor array was tested with different cinematographic and photographic film samples made of cellulose acetate, whose degradation state and acetic acid production was validated using the conventional technique (A-D strips). The presented array is suitable for remote monitoring large number of films in collections since, compared to the official technique, it has a lower detection limit (30 ppb vs. 500 ppb) and is much quicker in providing accurate acetic acid concentration in the film boxes (15 min vs. 24 h).

In this study, we report a novel way to produce carbon-based conductive inks for electronic and sensor technology applications. Carbonized lignin, obtained from the waste products of the Eucalyptus globulus tree paper industry, was used to produce a stable conductive ink. To this end, liquid-phase compositions were tested with different amounts of carbonized lignin powder to obtain an ink with optimal conductivity and rheological properties for different possible uses. The combination that showed the best properties, both regarding electrochemical properties and green compatibility of the materials employed, was cyclohexanone/cellulose acetate/carbonized lignin 5% (w/w), which was used to produce screen-printed electrodes. The electrodes were characterized from a structural and electrochemical point of view, resulting in an electrochemically active area of 0.1813 cm2, compared to the electrochemically active area of 0.1420 cm2 obtained by employing geometrically similar petroleum-based screen-printed electrodes and, finally, their performance was demonstrated for the quantification of uric acid, with a limit of detection of 0.3 μM, and their biocompatibility was assessed by testing it with the laccase enzyme and achieving a limit of detection of 2.01 μM for catechol as the substrate. The results suggest that the developed ink could be of great use in both sensor and electronic industries, reducing the overall ecological impact of traditionally used petroleum-based inks.

The RNA recognition motif (RRM), which is the most abundant RNA-binding motif in eukaryotes, is a well-structured domain of about 90 amino acids, yet the β2β3 hairpin, corresponding to strands 2 and 3 of the β-sheet, and the intervening loop make essential interactions with RNA in many RRM complexes. A series of small cyclic peptide mimics of the β2β3 hairpin of Rbfox2 protein that recognize the terminal loop of precursor miR-20b have been designed to investigate whether the full RNA-binding protein can be mimicked with a minimal structurally preorganized peptide. Within a small library of seven cyclic peptides, a peptide with low-micromolar affinity for the miR-20b precursor was found. NMR spectroscopy titration data suggest that this peptide specifically targets the apical loop of pre-miR-20b. This work shows that it is possible to mimic RNA-binding proteins with designed stable peptides, which provide a starting point for designing or evolving small peptide mimetics of RRM proteins.

This report documents the program and the outcomes of Dagstuhl Seminar 19342 ``Advances and Challenges in Protein-RNA Recognition, Regulation and Prediction''.

The RNA recognition motif (RRM) is the most common RNA binding domain across eukaryotic proteins. It is therefore of great value to engineer its specificity to target RNAs of arbitrary sequence. This was recently achieved for the RRM in Rbfox protein, where four mutations R118D, E147R, N151S, and E152T were designed to target the precursor to the oncogenic miRNA 21. Here, we used a variety of molecular dynamics-based approaches to predict specific interactions at the binding interface. Overall, we have run approximately 50 microseconds of enhanced sampling and plain molecular dynamics simulations on the engineered complex as well as on the wild-type Rbfox·pre-miRNA 20b from which the mutated systems were designed. Comparison with the available NMR data on the wild type molecules (protein, RNA, and their complex) served to establish the accuracy of the calculations. Free energy calculations suggest that further improvements in affinity and selectivity are achieved by the S151T replacement., Author summary RNA is an outstanding target for oncological intervention. Engineering the most common RNA binding motif in human proteins (called RRM) so as to bind to a specific RNA has an enormous pharmacological potential. Yet, it is highly non trivial to design RRM-bearing protein variants with RNA selectivity and affinity sufficiently high for clinical applications. Here we present an extensive molecular simulation study which shed light on the exquisite molecular recognition of the empirically-engineered complex between the RRM-bearing protein Rbfox and its RNA target pre-miR21. The simulations allow predicting a variant, the S151T, which may lead to further enhancement of selectivity and affinity for pre-miR21.