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As a consequence of the photovoltaic (PV) market expansion in the last 20 years, the cumulative global PV waste is expected to exponentially grow. A proper disposal of decommissioned PV panels is crucial for avoiding environmental risks and for recovering value-added materials. In this study, a Life Cycle Assessment (LCA) was performed in order to assess the environmental performance of a new recycling process for crystalline silicon (c-Si) PV panels, at the End of Life (EoL). The process was developed in the framework of the ReSiELP (Recovery of Silicon and other materials from the End-of-Life Photovoltaic Panels) project, aiming at recovering valuable resources from EoL PV c-Si modules and making the recovered materials readily available for different supply chains, in line with the principles of Circular Economy. A “gate to gate” approach was used to investigate two lines of activities: (i) the Recovery line, dedicated to the recovery of secondary raw materials from EoL c-Si PV panels, namely aluminium, copper, glass, silver and silicon, and (ii) the Glass reuse line, for the employment of the recovered glass in prefabricated building components (predalles slabs). The results highlight energy consumption, chemicals and transportation as the main hotspots of the ReSiELP process. For a comprehensive evaluation, the generated loads were compared with the potential environmental benefits gained thanks to the recovery of aluminium, at the largest extent. Overall, the LCA analysis showed that the investigated process is environmentally favorable, also when compared to other EoL PV panels recycling scenarios reported in literature.

A bicyclic undecapeptide of sequence cyclo-(Ala(1)-Pro(2)-Asp(3)-Glu(4)-Lys(5)-Ala(6)-Pro(7)-Asp(8)-Ser(9) -Glu(10))-cyclo-(10gamma --> 5varepsilon)-Gly(11), designed to mimic the calcium coordination site I of Calmodulin, has been synthesized and its conformation and calcium binding properties have been investigated by means of CD and nmr spectroscopy. The nmr analysis of the free peptide, carried out in DMSO and in TFE/H(2)O at different pH values, shows the presence in solution of one stable conformer, exhibiting trans configuration around both Proline residues. The nmr results in both solvents suggest for the molecule a rectangular shape constituted by two antiparallel beta-strands connected by two beta-turns. Interproton distances, evaluated by NOE contacts, have been used to obtain feasible models by means of Restrained Molecular Dynamic (RMD). The average models from RMD calculations, for both solvents, exhibit good analogies with Calmodulin site I. The model system, when compared with the reference system (Asp(20)-Glu(31) segment in CaM), shows similar dimensions and an effective superimposition of the respective sequence segments Ala(1)-Glu(4) and Thr(28)-Glu(31). The remaining segments of the model peptide exhibit a bending that is intermediate between that of the free and Ca(2+)-coordinated site I. CD spectra, recorded in TFE solutions, point to a 1:1 stoichiometry for the Ca(2+)-peptide complex, with an association constant of at least 1 x 10(5) M(-1).

In this paper we have reported a preliminary analysis of the functional and structural properties of a rationally designed DNA-binding peptide. Finger 4 is able to bind a DNA target sequence. More remarkably, the peptide sequence shows a high helical content, thus demonstrating the effectiveness of the Aib residue in inducing helical structures even in highly charged, water-solubles peptides.