LSRE-LCM - Artigos em Revistas Nacionais e de Circulação Internacional
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- Adsorption Behavior and Mechanism of Oxytetracycline on Rice Husk Ash: Kinetics, Equilibrium, and Thermodynamics of the ProcessPublication . Andrade, Christhel A.; Zambrano-Intriago, Luis Angel; Oliveira, Nelson S.; Vieira, Judite S.; Quiroz-Fernández, Luis Santiago; Rodríguez-Díaz, Joan ManuelThe main objective of the present study is to determine the kinetics, thermodynamics, and adsorption mechanism of the oxytetracycline (OTC) on rice husk ash (RHA). The adsorbent was characterized by scanning electronic microscopy, Fourier transform infrared spectroscopy, and nitrogen physisorption. Batch studies were carried out to evaluate the influence of the adsorbent dose, initial concentration, contact time, temperature, and initial pH. RHA was characterized as having heterogeneous, fibrous, and porous particles, consisting predominantly of silica. The removal of OTC depends on the pH of the medium, which is favored at acid pH values. The kinetic data followed the Bangham model, which indicated an OTC diffusion in the pores of RHA, although this was not the only process, as demonstrated through the use of the Weber-Morris model (IPD model). The Sips isotherm best represents the experimental results of the equilibrium study. It was found that the adsorption process was spontaneous and endothermic. The highest adsorption capacity was found at a pH in the range of 4–6, when the OTC is in its zwitterion form and the surface of the RHA is positively charged, thus permitting electrostatic interactions and the formation of hydrogen bonds between the adsorbent and adsorbate molecules. These findings demonstrate the potential of rice husk ash to remove oxytetracycline from water.
- Are There Lipid Membrane-Domain Subtypes in Neurons with Different Roles in Calcium Signaling?Publication . Samhan-Arias, Alejandro K.; Poejo, Joana; Marques-da-Silva, Dorinda; Martínez-Costa, Oscar H.; Gutierrez-Merino, CarlosLipid membrane nanodomains or lipid rafts are 10–200 nm diameter size cholesterol- and sphingolipid-enriched domains of the plasma membrane, gathering many proteins with different roles. Isolation and characterization of plasma membrane proteins by differential centrifugation and proteomic studies have revealed a remarkable diversity of proteins in these domains. The limited size of the lipid membrane nanodomain challenges the simple possibility that all of them can coexist within the same lipid membrane domain. As caveolin-1, flotillin isoforms and gangliosides are currently used as neuronal lipid membrane nanodomain markers, we first analyzed the structural features of these components forming nanodomains at the plasma membrane since they are relevant for building supramolecular complexes constituted by these molecular signatures. Among the proteins associated with neuronal lipid membrane nanodomains, there are a large number of proteins that play major roles in calcium signaling, such as ionotropic and metabotropic receptors for neurotransmitters, calcium channels, and calcium pumps. This review highlights a large variation between the calcium signaling proteins that have been reported to be associated with isolated caveolin-1 and flotillin-lipid membrane nanodomains. Since these calcium signaling proteins are scattered in different locations of the neuronal plasma membrane, i.e., in presynapses, postsynapses, axonal or dendritic trees, or in the neuronal soma, our analysis suggests that different lipid membrane-domain subtypes should exist in neurons. Furthermore, we conclude that classification of lipid membrane domains by their content in calcium signaling proteins sheds light on the roles of these domains for neuronal activities that are dependent upon the intracellular calcium concentration. Some examples described in this review include the synaptic and metabolic activity, secretion of neurotransmitters and neuromodulators, neuronal excitability (long-term potentiation and long-term depression), axonal and dendritic growth but also neuronal cell survival and death.
- Bidentate Urea Derivatives of p-tert-Butyldihomooxacalix[4]arene: Neutral Receptors for Anion ComplexationPublication . Marcos, Paula M.; Teixeira, Filipa A.; Segurado, Manuel A. P.; Ascenso, José R.; Bernardino, Raul J.; Michel, Sylvia; Hubscher-Bruder, VéroniqueThree new bidentate ureidodihomooxacalix[4]- arene derivatives (phenyl 5a, n-propyl 5b, and tert-butyl 5c) were synthesized in four steps from the parent compound ptert- butyldihomooxacalix[4]arene and obtained in the cone conformation, as shown by NMR studies. The binding ability of these neutral receptors toward spherical, linear, trigonal planar, and tetrahedrical anions was assessed by 1H NMR and UV-vis titrations. The structures and complexation energies of some complexes were also studied by DFT methods. The data showed that the association constants are strongly dependent on the nature of the substituent (aryl/alkyl) at the urea moiety. In general, for all the receptors, the association constants decrease with decrease of anion basicity. Ph-urea 5a is the best anion receptor, showing the strongest complexation for F- (log Kassoc = 3.10 in CDCl3) and also high binding affinity for the carboxylates AcO- and BzO-. Similar results were obtained by UV-vis studies and were also corroborated by DFT calculations.
- Cardiolipin Membranes Promote Cytochrome c Transformation of Polycyclic Aromatic Hydrocarbons and Their In Vivo MetabolitesPublication . Lopes, João; Marques-da-Silva, Dorinda; Videira, Paula A.; Samhan-Arias, Alejandro K.; Lagoa, RicardoThe catalytic properties of cytochrome c (Cc) have captured great interest in respect to mitochondrial physiology and apoptosis, and hold potential for novel enzymatic bioremediation systems. Nevertheless, its contribution to the metabolism of environmental toxicants remains unstudied. Human exposure to polycyclic aromatic hydrocarbons (PAHs) has been associated with impactful diseases, and animal models have unveiled concerning signs of PAHs’ toxicity to mitochondria. In this work, a series of eight PAHs with ionization potentials between 7.2 and 8.1 eV were used to challenge the catalytic ability of Cc and to evaluate the effect of vesicles containing cardiolipin mimicking mitochondrial membranes activating the peroxidase activity of Cc. With moderate levels of H2O2 and at pH 7.0, Cc catalyzed the oxidation of toxic PAHs, such as benzo[a]pyrene, anthracene, and benzo[a]anthracene, and the cardiolipin-containing membranes clearly increased the PAH conversions. Our results also demonstrate for the first time that Cc and Cc–cardiolipin complexes efficiently transformed the PAH metabolites 2-hydroxynaphthalene and 1-hydroxypyrene. In comparison to horseradish peroxidase, Cc was shown to reach more potent oxidizing states and react with PAHs with ionization potentials up to 7.70 eV, including pyrene and acenaphthene. Spectral assays indicated that anthracene binds to Cc, and docking simulations proposed possible binding sites positioning anthracene for oxidation. The results give support to the participation of Cc in the metabolism of PAHs, especially in mitochondria, and encourage further investigation of the molecular interaction between PAHs and Cc.
- Humic acid aggregates with laccase and decreases the performance of the enzyme catalytic systems through various mechanismsPublication . Lopes, João; Marques-da-Silva, Dorinda; Peralta, Cláudia; Rodrigues, Joaquim Rui; Vaz, Daniela; Lagoa, RicardoLaccases are among the best-rated enzymes for industrial and environmental applications, yet their use in bioremediation is limited by interference from environmental components like humic acid (HA). This study evaluated HA impact on the oxidation of 2,2 ′-azino-bis-(3-ethylbenzothiazoline-6-sulphonate (ABTS) and two model pollutants — anthracene and methyl orange — by laccase( mediator) systems. HA consistently diminished conversion rates, with EC50 values between 5 and 51 mg/L suggesting diverse inhibitory mechanisms. We investigated potential mechanisms including substrate sequestration, radical quenching, and chelation of laccase coppers by HA. Incubations with free and immobilized HA showed that adsorption can impede anthracene degradation, at least at high concentrations, but not methyl orange. Using chemically generated ABTS radical and azide-blocked enzyme, it was demonstrated that HA scavenges free radicals produced by laccase, though this alone did not fully explain the observed interference with catalysis. Further assays with metal chelator and added copper or calcium ruled out HA binding to the laccase metal centers. Instead, data from molecular docking, f luorescence, light scattering, and microscopy revealed that HA forms micrometer-scale aggregates with laccase that encapsulate the enzyme. This newly identified mechanism likely applies broadly to laccase-based systems and must be considered in applications involving aqueous media containing humic substances.
- Molecular Dissection of Escherichia coli CpdB: Roles of the N Domain in Catalysis and Phosphate Inhibition, and of the C Domain in Substrate Specificity and Adenosine InhibitionPublication . López-Villamizar, Iralis; Cabezas, Alicia; Pinto, Rosa María; Canales, José; Ribeiro, João Meireles; Rodrigues, Joaquim Rui; Costas, María Jesús; Cameselle, José CarlosCpdB is a 3′-nucleotidase/2′ 3′-cyclic nucleotide phosphodiesterase, active also with rea-sonable efficiency on cyclic dinucleotides like c-di-AMP (3′,5′-cyclic diadenosine monophosphate) and c-di-GMP (3′,5′-cyclic diadenosine monophosphate). These are regulators of bacterial physi-ology, but are also pathogen-associated molecular patterns recognized by STING to induce IFN-β response in infected hosts. The cpdB gene of Gram-negative and its homologs of gram-positive bacteria are virulence factors. Their protein products are extracytoplasmic enzymes (either periplas-mic or cell–wall anchored) and can hydrolyze extracellular cyclic dinucleotides, thus reducing the innate immune responses of infected hosts. This makes CpdB(-like) enzymes potential targets for novel therapeutic strategies in infectious diseases, bringing about the necessity to gain insight into the molecular bases of their catalytic behavior. We have dissected the two-domain structure of Escherichia coli CpdB to study the role of its N-terminal and C-terminal domains (CpdB_Ndom and CpdB_Cdom). The specificity, kinetics and inhibitor sensitivity of point mutants of CpdB, and truncated proteins CpdB_Ndom and CpdB_Cdom were investigated. CpdB_Ndom contains the catalytic site, is inhibited by phosphate but not by adenosine, while CpdB_Cdom is inactive but contains a substrate-binding site that determines substrate specificity and adenosine inhibition of CpdB. Among CpdB substrates, 3′-AMP, cyclic dinucleotides and linear dinucleotides are strongly dependent on the CpdB_Cdom binding site for activity, as the isolated CpdB_Ndom showed much-diminished activity on them. In contrast, 2′,3′-cyclic mononucleotides and bis-4-nitrophenylphosphate were actively hydrolyzed by CpdB_Ndom, indicating that they are rather independent of the CpdB_Cdom binding site.
- 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.