63 research outputs found

    An in-and-out-the-lab Raman spectroscopy study on street art murals from Reggio Emilia in Italy

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    The street art murals ‘The Big Mother’ by Gola Hundun, the ‘Big Sacral Bird’ by Kenor, the ‘Oriental Carpet” by H101 and “The Economy Subdues You” by Zosen, belonging to the Cooperative Popular Houses of Mancasale and Coviolo in Reggio Emilia (Italy), were investigated by the use of various mobile Raman spectrometers coupled to different lasers and by micro-Raman spectroscopy on selected samples. The study was made necessary by the evident fading of many colours, despite the young age of the paintings, realized in 2010. The first step of the investigation, realized by the on-site campaign, was the identification of the materials, and in particular of the dyes. The main chromophores were identified as polycyclic, monoazo- and disazo- organic pigments, with inorganic compounds as bismuth vanadate (BiVO4) together with the extensive presence of rutile (TiO2). The second step was devoted to the study of the degradation mechanism affecting the colourful layers of the murals. It required the use of laboratory micro-spectrometers and was carried out on a reduced set of samples, selected during the in-situ campaign. This combination of on-site and laboratory Raman spectroscopy allowed the obtaining of the complete identification of the palette used by the different artists in a single day of measurements, in a complete non-destructive day. In addition, it was possible to minimize the number of samples required for the study of the degradation process. Graphical abstract: [Figure not available: see fulltext.

    A Chaperone Trap Contributes to the Onset of Cystic Fibrosis

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    Protein folding is the primary role of proteostasis network (PN) where chaperone interactions with client proteins determine the success or failure of the folding reaction in the cell. We now address how the Phe508 deletion in the NBD1 domain of the cystic fibrosis (CF) transmembrane conductance regulator (CFTR) protein responsible for cystic fibrosis (CF) impacts the binding of CFTR with cellular chaperones. We applied single ion reaction monitoring mass spectrometry (SRM-MS) to quantitatively characterize the stoichiometry of the heat shock proteins (Hsps) in CFTR folding intermediates in vivo and mapped the sites of interaction of the NBD1 domain of CFTR with Hsp90 in vitro. Unlike folding of WT-CFTR, we now demonstrate the presence of ΔF508-CFTR in a stalled folding intermediate in stoichiometric association with the core Hsps 40, 70 and 90, referred to as a ‘chaperone trap’. Culturing cells at 30 C resulted in correction of ΔF508-CFTR trafficking and function, restoring the sub-stoichiometric association of core Hsps observed for WT-CFTR. These results support the interpretation that ΔF508-CFTR is restricted to a chaperone-bound folding intermediate, a state that may contribute to its loss of trafficking and increased targeting for degradation. We propose that stalled folding intermediates could define a critical proteostasis pathway branch-point(s) responsible for the loss of function in misfolding diseases as observed in CF
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