Dataset Information

Toward a Reversible Consolidation of Paper Materials Using Cellulose Nanocrystals.

ABSTRACT: An innovative consolidation strategy for degraded paper is presented based on the reversible application of cellulose nanocrystals as sustainable fillers to reinforce mechanical properties and resistance to further degradation. The compatibility and efficacy of the proposed consolidation treatment are assessed first on pure cellulose paper, used as a model, by reliable techniques such as field emission scanning electron microscopy, atomic force microscopy, tensile tests, X-ray powder diffraction, and Fourier transform infrared spectroscopy, evidencing the influence of the surface functionalization of nanocellulose on the consolidation and protection effects. Then, the consolidation technique is applied to real aged paper samples from Breviarium romanum ad usum Fratrum Minorum S.P. (1738), demonstrating the promising potential of the suggested approach. Amperometric measurements, carried out with a smart electrochemical tool developed in our laboratory, demonstrate the reversibility of the proposed treatment by removal of the nanocrystalline cellulose from the paper surface with a suitable cleaning hydrogel. This completely new feature of the consolidation treatment proposed here satisfies a pivotal requisite in cultural heritage conservation because the methodological requirement for the ″reversibility″ of any conservation measure is a fundamental goal for restorers. A paper artifact, in fact, is subject to a number of natural and man-made hazards, inducing continuous degradation. With time, monitoring and consolidation actions need to be often performed to ensure conservation, and this tends to modify the status quo and compromise the artifact integrity. Removable treatments can potentially avoid erosion of the artifact integrity.

SUBMITTER: Operamolla A

PROVIDER: S-EPMC8461603 | biostudies-literature |

REPOSITORIES: biostudies-literature

ACCESS DATA

Similar Datasets

Project description:Membrane proteins are very important for all living cells, being involved in respiration, photosynthesis, cellular uptake and signal transduction, amongst other vital functions. However, less than 300 unique membrane protein structures have been determined to date, often due to difficulties associated with the growth of sufficiently large and well-ordered crystals. This work has been focused on showing the first proof of concept for using membrane protein nanocrystals and microcrystals for high-resolution structure determination. Upon determining that crystals of the membrane protein Photosystem I, which is the largest and most complex membrane protein crystallized to date, exist with only 100 unit cells with sizes of less than 200 nm on an edge, work was done to develop a technique that could exploit the growth of the Photosystem I nanocrystals and microcrystals. Femtosecond X-ray protein nanocrystallography was developed for use at the first high-energy X-ray free electron laser, the LCLS at SLAC National Accelerator Laboratory, in which a liquid jet brought fully-hydrated Photosystem I nanocrystals into the interaction region of the pulsed X-ray source. Diffraction patterns were recorded from millions of individual PSI nanocrystals and data from thousands of different, randomly oriented crystallites were integrated using Monte Carlo integration of the peak intensities. The short pulses (?70fs) provided by the LCLS allowed the possibility to collect the diffraction data before the onset of radiation damage, exploiting the diffract-before-destroy principle. During the initial experiments at the AMO beamline using 6.9-? wavelength, Bragg peaks were recorded to 8.5-? resolution, and an electron-density map was determined that did not show any effects of X-ray-induced radiation damage [94]. Many additional techniques still need to be developed to explore the femtosecond nanocrystallography technique for experimental phasing and time-resolved X-ray crystallography experiments. The first proof-of-principle results for the femtosecond nanocrystallography technique indicate the incredible potential of the technique to offer a new route to the structure determination of membrane proteins.

Dataset Information

Toward a Reversible Consolidation of Paper Materials Using Cellulose Nanocrystals.

Similar Datasets

OmicsDI is part of the ELIXIR infrastructure

Tweets