A multi-element psychosocial intervention for early psychosis (GET UP PIANO TRIAL) conducted in a catchment area of 10 million inhabitants: study protocol for a pragmatic cluster randomized controlled trial

Multi-element interventions for first-episode psychosis (FEP) are promising, but have mostly been conducted in non-epidemiologically representative samples, thereby raising the risk of underestimating the complexities involved in treating FEP in 'real-world' services

Conformational study and Hydrogen bonds detection on Elastin-related poly-peptides using X-ray Photoelectron Spectroscopy, XPS

The chemical bonds of the pentapeptide sequence of elastin ValGlyGlyValGly (VGGVG), both in its monomer and polymer forms, were correlated with their XPS spectra through a well-established curve-fitting procedure. To aid in this correlation, the C1s, O1s, and N1s chemical shifts of the Boc-VGGVG-OEt, were validated by theoretical calculations, performed in the framework of the Koopman approximation of HF/6-31G molecular orbitals, leading to the "preferred" conformation of the protected monomer. Then the same curve-fitting procedure was adopted for interpreting the XPS spectra of the polypentapeptide as a powder, and the XPS results obtained both for monomer and polymer compounds were compared with those obtained by FT-IR. The polymer was then analyzed after deposition onto a silicon substrate, Si(100), either from methanol or water suspensions and the presence of hydrogen bonds was detected at the polymer/substrate interface and between the polymer chains. The "surface rearrangement" that could be inferred from XPS results strongly confirms that derived from AFM images previously obtained under the same experimental conditions. In particular, the observed amyloid conformation is stabilized by hydrogen bonds to water molecules included in the structure while the formation of the beaded string structure observed in deposits from methanolic suspension is probably mediated by hydrogen bonds to the hydrated silicon surface

Investigating the amyloidogenic nanostructured sequences of elastin: sequence encoded by exon 28 of human tropoelastin gene

In this paper we demonstrate that the sequence encoded by exon 28 (EX28) of human tropoelastin gene is able to give amyloid-like fibrils. CD (circular dichroism) in solution and solid-state FTIR (Fourier transform infrared spectroscopy) spectroscopies have shown the presence of beta-sheet conformation. At the supramolecular level the fibers formed by EX28 peptide were investigated by AFM (atomic force microscopy) and ESEM (environmental scanning electron microscopy). A very big left-handed helix, 100 mum long, is visible together with aggregates of different sizes, some of them being constituted by helically interwoven fibers. Furthermore, an additional AFM image of EX28 is shown where the ultrastructure found is somewhat reminiscent of a more or less retiform film. These findings should be useful for designing proper elastin-inspired biomaterials

‘Transformation of amyloid-like fibres, formed from an elastin-based biopolymer, into hydrogel: an XPS and AFM study’

Previous studies have revealed the propensity of elastin-based biopolymers to form amyloid-like fibers when dissolved in water. These are of interest when considered as "ancestral units" of elastin in which they represent the simplest sequences in the hydrophobic regions of the general type XxxGlyGlyZzzGly (Xxx, Zzz = Val, Leu). We normally refer to these biopolymers based on elastin or related to elastin units as "elastin-like polypeptides". The requirement of water for the formation of amyloids seems quite interesting and deserves investigation, the water representing the natural transport medium in human cells. As a matter of fact, the "natural" supramolecular organization of elastin is in the form of beaded-string-like filaments and not in the form of amyloids whose "in vivo" deposition is associated with some important human diseases. Our work is directed, therefore, to understanding the mechanism by which such hydrophobic sequences form amyloids and any conditions by which they might regress to a non-amyloid filament. The elastin-like sequence here under investigation is the ValGlyGly ValGly pentapeptide that has been previously analyzed both in its monomer and polymer form. In particular, we have focused our investigation on the apparent stability of amyloids formed from poly(ValGlyGlyValGly), and we have observed these fibers evolving to a hydrogel after prolonged aging in water. We will show how atomic force microscopy can be combined with X-ray photoelectron spectroscopy to gain an insight into the spontaneous organization of an elastin-like polypeptide driven by interfacial interactions. The results are discussed also in light of fractal-like assembly and their implications from a biomedical point of view

Production scheduling using multi-objective optimization and cluster approaches

Production scheduling is a crucial task in the manufacturing process. In this way, the managers need to make decisions about the jobs production schedule. However, this task is not simple to perform, often requiring complex software tools and specialized algorithms to find the optimal solution. This work considers a multi-objective optimization algorithm to explore the production scheduling performance measure in order to help managers in decision making related to jobs attribution in a set of parallel machines. For this, five important production scheduling performance measures (makespan, tardiness and earliness time, number of tardy and early jobs) were combined into three objective functions and the Pareto front generated was analyzed by cluster techniques. The results presented different combinations to optimize the production process, providing to the manager different possibilities to prioritize the objectives considered.This work has been supported by FCT – Funda¸c˜ao para a Ciência e Tecnologia within the R&D Units Project Scope: UIDB/00319/2020 and EXPL/EMESIS/1224/2021. Beatriz Flamia Azevedo is supported by FCT Grant Reference SFRH/BD/07427/2021.info:eu-repo/semantics/publishedVersio