LSRE-LCM - Artigos em Revistas Nacionais e de Circulação Internacional
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Percorrer LSRE-LCM - Artigos em Revistas Nacionais e de Circulação Internacional por Objetivos de Desenvolvimento Sustentável (ODS) "09:Indústria, Inovação e Infraestruturas"
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- The Effect of a Naturally Ventilated Roof on the Thermal Behaviour of a Building under Mediterranean Summer ConditionsPublication . Ramos, João; Aires, LuisWith the increasing cost associated with energy consumption, climate change and the greater awareness of the population to issues related to energy and environmental efficiency, energy conservation in buildings has been encouraged, along with the development of several solutions based on a more sustainable construction. Building cooling is the most challenging issue in the Mediterranean climate. The roof is one of the main elements of the building’s opaque envelope, where the choice of materials and the implementation of appropriate passive technologies determine the thermal performance of a building. The present work aims to assess the impact of natural ventilation of a roof cavity on the thermal environment of a dwelling house under Mediterranean summer conditions. An experimental study was developed in a small-scale prototype of a typical dwelling house, comprising a ceramic tile roof with vented eaves and insulated sub-tile panels according to the construction solution of the Humbelino Monteiro SA company. The thermal performance of this roof solution was assessed under real climatic conditions based on continuous measurements of the air velocity inside the air gap, the temperature of the air and the surface temperature of all roof layers. Weather conditions were also monitored continuously. Connected with the heat transfer mechanisms, the obtained temperature and air velocity profiles data were analysed and discussed.
- Serum-PEG and BSA-PEG hydrogels as advanced platforms for evaluating plasma protein bindingPublication . Coelho, Carlos D.F.; Paiva, Victor S.; Almeida, Zaida L.; Jesus, João A.; Marteleira, Madalena; Ramos, Cristiana V.; Cruz, Pedro F.; Costa, Telma; Moura, Carla S.; Trindade, Daniela; Brito, Rui M.M.; Lagoa, Ricardo; Vaz, Daniela C.; Moreno, Maria JoãoThe binding of bioactive compounds to proteins is critical for their availability and ADME/Tox profile. Specifically, binding to serum proteins affects both the distribution and elimination of drugs, while permeation through protein-enriched matrices, such as skin, is also influenced by protein interactions. Although several methods exist to evaluate ligand-protein binding, they often fail to replicate the high protein concentrations and molecular crowding conditions found in vivo. In this study, we investigate the use of protein-PEG hydrogels with low crosslinking density as 3D matrices to quantify ligand-protein affinity. Two types of hydrogels were developed: one using bovine serum albumin (BSA) and a more physiologically relevant one using serum. BSA was chosen as a model protein due to its similarity to human serum albumin. The hydrogels were characterized for swelling, stability, mechanical properties, and porosity, and the structural integrity of BSA within the hydrogel was confirmed using circular dichroism, 1H NMR and fluorescence spectroscopy. To assess protein functionality, we evaluated the binding affinity of various ligands, including a homologous series of fluorescent amphiphiles with different hydrophobicity (NBD-Cn, where n = 4, 6, and 8), two pesticides (malathion and chlorpyrifos), and six pharmaceutical drugs (acetaminophen, chlorpromazine, diclofenac, labetalol, salicylic acid, and verapamil). Our results demonstrated that the structural and functional properties of BSA remained intact within the hydrogel, and the large mesh size allowed for rapid and selective ligand binding. A comparison of BSA and serum hydrogels confirmed the major role of serum albumin in ligand binding, while highlighting some differences between cationic and anionic ligands. Altogether, these hydrogels offer an effective and reliable 3D platform for the fast and accurate evaluation of plasma protein binding of drugs and other bioactive compounds.