RESUMO
In this paper, we report structural, electronic and optical properties of cubane (C8H8) and cubanoids (cubane-like molecules) using Density Functional Theory (DFT). The cubanoids are cubanes for which Carbon atoms have been substituted by Nitrogen (N), Phosphorus (P), Boron (B), Silicon (Si), Arsenic (As), Antimony (Sb) or Bismuth (Bi) atoms. These molecules presented exceptional stability with several different symmetry point groups, being the majority Td. All calculated vibrational frequencies are positive for any studied molecules indicating that all these structures are in a stable state. The HOMO-LUMO gaps and DOS were calculated converged towards to values between 1.87 eV and 5.61 eV, actually showing promising electronic properties (Just for comparison, the cubane energy gap is 7.50 eV). The optical absorptions were also calculated for the cubanoid structure using the Time-Dependent Density Functional Theory (TD-DFT). Their dependence on the wavelength is analyzed, where five of theses structures absorb on the visible region. Finally, the extrapolation of thermodynamic properties indicates that these cubanoid could be potentially synthesized spontaneously, where four structures, the synthesis would occur for temperatures below 400 K, while for Si4Bi4H4 structure, the synthesis would occur at room temperature.
Assuntos
Teoria Quântica , Vibração , Teoria da Densidade Funcional , Modelos Moleculares , Espectroscopia de Infravermelho com Transformada de Fourier , TermodinâmicaRESUMO
The objective of the present study was to determine the anxiety and stress levels of liver transplant candidates during the preoperative period. A cross-sectional, prospective study was conducted on 52 liver transplantation candidates seen at a specialized public hospital outpatient clinic in the interior of the state of São Paulo, Brazil. Data were collected from November 2014 to April 2015 using a self-applicable questionnaire for the assessment of anxiety (State-Trait Anxiety Inventory, short version) and stress (Perceived Stress Scale), in addition to sociodemographic and clinic characterization. The mean (±SD) anxiety level detected was 23.06 ± 5.51 points, with 1.92% of the subjects showing minimum levels (0 to 12 points), 59.62% a medium level (12 to 24 points), 36.54% a moderate level (24 to 36 points), and 1.92% a severe level (36 to 48 points) of anxiety. The mean level on the stress scale was 12.10 ± 5.62 points, with 7.69% of the subjects showing high stress levels. When individuals with good and poor stress levels were compared, a significant difference was observed between them (P = .0004). The Spearman correlation test showed that the higher the stress, the higher the levels of anxiety (r = 0.4258), P < .0001. The present study contributes to the analysis of the mental health of liver transplantation candidates in view of the need for interventions for the improvement of anxiety and stress levels since the waiting period for the organ generates emotional changes that can affect the quality of life of the patient and the success of this complex therapeutic modality.
Assuntos
Ansiedade/psicologia , Cirrose Hepática/psicologia , Transplante de Fígado/psicologia , Estresse Psicológico/psicologia , Adolescente , Adulto , Idoso , Brasil , Estudos Transversais , Feminino , Hepatite Viral Humana/complicações , Humanos , Cirrose Hepática/etiologia , Cirrose Hepática/cirurgia , Cirrose Hepática Alcoólica/psicologia , Cirrose Hepática Alcoólica/cirurgia , Masculino , Saúde Mental , Pessoa de Meia-Idade , Período Pré-Operatório , Estudos Prospectivos , Qualidade de Vida , Inquéritos e Questionários , Listas de Espera , Adulto JovemRESUMO
OBJECTIVE: The goal of this study was to evaluate the sleep quality and daytime sleepiness of patients eligible for liver transplants. METHODS: A cross-sectional prospective study was conducted on liver transplant candidates from a transplant center in the interior of São Paulo State. The Pittsburgh Sleep Quality Index and Epworth Sleepiness Scale questionnaires were applied to obtain demographic and clinical characteristics and to assess sleep quality and daytime sleepiness. RESULTS: The mean (±SD) score on the Epworth Sleepiness Scale of the 45 liver transplantation candidates was 7.00 ± 2.83 points, with 28.89% having scores >10 points, indicating excessive daytime sleepiness. The mean score on the Pittsburgh Sleep Quality Index was 6.64 ± 4.95 points, with 60% of the subjects showing impaired sleep quality, with scores >5 points. The average sleep duration was 07:16 h. Regarding sleep quality self-classification, 31.11% reported poor or very poor quality. It is noteworthy that 73.33% of patients had to go to the bathroom, 53.33% woke up in the middle of the night, and 40.00% reported pain related to sleeping difficulties. Comparison of subjects with good and poor sleep quality revealed a significant difference in time to sleep (P = .0002), sleep hours (P = .0003), and sleep quality self-classification (P = .000072). CONCLUSION: Liver transplant candidates have a compromised quality of sleep and excessive daytime sleepiness. In clinical practice, we recommend the evaluation and implementation of interventions aimed at improving the sleep and wakefulness cycle, contributing to a better quality of life.
Assuntos
Hepatopatias/complicações , Transplante de Fígado , Transtornos do Sono-Vigília/etiologia , Sono , Adulto , Estudos Transversais , Feminino , Humanos , Masculino , Pessoa de Meia-Idade , Estudos Prospectivos , Qualidade de Vida , Transtornos do Sono-Vigília/epidemiologia , Inquéritos e QuestionáriosRESUMO
We report differential and integral elastic cross sections for low-energy electron collisions with CF3Cl, CF2Cl2, and CFCl3 molecules for energies ranging from 0.1 eV to 30 eV. The calculations were performed using the Schwinger multichannel method with pseudopotentials in the static-exchange and static-exchange plus polarization approximations. The influence of the permanent electric dipole moment on the cross sections was included using the Born closure scheme. A very good agreement between our calculations and the experimental results of Jones [J. Chem. Phys. 84, 813 (1986)], Mann and Linder [J. Phys. B 25, 1621 (1992); 25, 1633 (1992)] and Hoshino et al. [J. Chem. Phys. 138, 214305 (2013)] was found. We also compare our results with the calculations of Beyer et al. [Chem. Phys. 255, 1 (2000)] using the R-matrix method, where we find good agreement with respect to the location of the resonances, and with the calculations of Hoshino et al. using the independent atom method with screening corrected additivity rule, where we find qualitative agreement at energies above 20 eV. Additional electronic structure calculations were carried out in order to help in the interpretation of the scattering results. The stabilization the lowest σ(∗) resonance due to the exchange of fluorine by chlorine atoms (halogenation effect) follows a simple linear relation with the energy of the lowest unoccupied molecular orbitals and can be considered as a signature of the halogenation effect.
RESUMO
Aquatic ecosystems are under constant risk due to industrial, agricultural, and urban activities, compromising water quality and preservation of aquatic biota. The assessment of toxicological impacts caused by pollutants to aquatic environment using biomarker measurements in fish can provide reliable data to estimate sublethal effects posed by chemicals in contaminated areas. In this study, fish (Astyanax sp. and Danio rerio) exposed to agricultural and urban effluents at the Vacacaí River, Brazil, were tested for potential signs of aquatic contamination. This river comprehends one of the main watercourses of the Brazilian Pampa, a biome with a large biodiversity that has been neglected in terms of environmental and social-economic development. Sites S1 and S2 were chosen by their proximity to crops and wastewater discharge points, while reference site was located upstream of S1 and S2, in an apparently non-degraded area. Fish muscle and brain tissues were processed for determination of acetylcholinesterase as well as oxidative stress-related biomarkers. The results showed signs of environmental contamination, hallmarked by significant changes in cholinesterase activity, expression of metallothionein, antioxidant enzymes, glutathione levels, and activation of antioxidant/cell stress response signaling pathways in fish exposed to contaminated sites when compared to reference. Based on these results, it is evidenced that urban and agricultural activities are posing risk to the environmental quality of water resources at the studied area. It is also demonstrated that cell stress biomarkers may serve as important tools for biomonitoring and development of risk assessment protocols in the Pampa biome.
Assuntos
Characidae/metabolismo , Estresse Oxidativo , Poluentes Químicos da Água/toxicidade , Proteínas de Peixe-Zebra/metabolismo , Peixe-Zebra/metabolismo , Acetilcolinesterase/metabolismo , Agricultura , Animais , Biomarcadores/metabolismo , Brasil , Catalase/metabolismo , Ecossistema , Feminino , Glutationa Peroxidase/metabolismo , Glutationa Transferase/metabolismo , Masculino , Metalotioneína/metabolismo , Músculo Esquelético/efeitos dos fármacos , Músculo Esquelético/enzimologia , Rios/química , Compostos de Sulfidrila/metabolismo , Superóxido Dismutase/metabolismo , Águas Residuárias/química , Águas Residuárias/toxicidade , Poluentes Químicos da Água/análise , Qualidade da ÁguaRESUMO
Digestive carbohydrases are present in many species of hematophagous Arthropoda, including ticks. In this work, Amblyomma cajennense (Ixodidae) midgut digestive carbohydrases were tracked with different substrates, resulting in the identification of a chitinase and an N-acetyl-ß-glucosaminidase and the first description of a digestive α-L-fucosidase in ticks. α-L-fucosidases are involved in various physiological processes, and digestive α-L-fucosidases have been shown to be present in other types of organisms. Amblyomma cajennense α-L-fucosidase activity was isolated using acidic and salting-out precipitations and chromatographic steps in hydrophobic and cation-exchange columns. The specificity of the isolated activity as an α-L-fucosidase was confirmed by the hydrolysis of 4-methylumbelliferyl α-L-fucopyranoside and the natural substrate fucoidan and the inhibition by fucose and deoxyfuconojirimycin. The isolated activity of α-L-fucosidase forms oligomers with molecular mass of 140 kDa or 150 kDa as determined by gel filtration and non-reducing SDS-PAGE, respectively. This particular fucosidase has an optimum pH of 5.3, is stable even at high temperatures (stable for at least 2h at 50 °C), has a Km of 45 µM to the substrate 4-methylumbelliferyl α-L-fucopyranoside and IC 50% of 327 µM to fucose and 42 pM to deoxyfuconojirimycin. The presence of digestive fucosidases in hematophagous Arthropoda may be related to defence mechanisms against host-parasite interactions.
Assuntos
Acetilglucosaminidase/metabolismo , Metabolismo dos Carboidratos , Quitinases/metabolismo , Carrapatos/metabolismo , alfa-L-Fucosidase/metabolismo , Animais , Digestão , Feminino , Coelhos , alfa-L-Fucosidase/isolamento & purificaçãoRESUMO
Insect chymotrypsins are distinctively sensitive to plant protein inhibitors, suggesting that they differ in subsite architecture and hence in substrate specificities. Purified digestive chymotrypsins from insects of three different orders were assayed with internally quenched fluorescent oligopeptides with three different amino acids at P1 (Tyr, Phe, and Leu) and 13 amino acid replacements in positions P1', P2, and P3. The binding energy (DeltaG(s), calculated from K(m) values) and the activation energy (DeltaG(T)++, determined from k(cat)/K(m) values) were calculated. The hydrophobicities of each subsite were calculated from the efficiency of hydrolysis of the different amino acid replacements at that subsite. The results showed that except for S1, the other subsites (S2, S3, and S1') vary among chymotrypsins. This result contrasts with insect trypsin data that revealed a trend along evolution, putatively associated with resistance to plant inhibitors. In spite of those differences, the data suggested that in lepidopteran chymotrypsins S2 and S1' bind the substrate ground state, whereas only S1' binds the transition state, supporting aspects of the present accepted mechanism of catalysis.
Assuntos
Quimotripsina/metabolismo , Baratas/enzimologia , Besouros/enzimologia , Lepidópteros/enzimologia , Animais , Sítios de Ligação , Catálise , Quimotripsina/isolamento & purificação , Trato Gastrointestinal/enzimologia , Interações Hidrofóbicas e Hidrofílicas , Especificidade por SubstratoRESUMO
Trypsins have high sequence similarity, although the responses of insect trypsins to chemical and natural inhibitors suggest they differ in specificities. Purified digestive trypsins from insects of four different orders were assayed with internally quenched fluorescent oligopeptides with two different amino acids at P1 (Arg/Lys) and 15 amino acid replacements in positions P1', P2', P2, and P3. The binding energy (deltaG(s), calculated from Km values) and the activation energy (deltaG(T)(double dagger), determined from kcat/Km values) were calculated. Dictyoptera, Coleoptera and Diptera trypsins hydrolyze peptides with Arg at P1 at least 3 times more efficiently than peptides with Lys at P1, whereas Lepidoptera trypsins have no preference between Arg and Lys at that position. The hydrophobicities of each subsite were calculated from the efficiency of hydrolysis of the different amino acid replacements at that subsite. The results suggested that insect trypsin subsites become progressively more hydrophobic along evolution. Apparently, this is an adaptation to resist plant protein inhibitors, which usually have polar residues at their reactive sites. Results also suggested that, at least in lepidopteran trypsins, S3, S2, S1', and S2' significantly bind the substrate ground state, whereas in the transition state only S1' and S2' do that, supporting aspects of the presently accepted mechanism of trypsin catalysis. Homology modeling showed differences among those trypsins that may account for the varied kinetic properties.
Assuntos
Proteínas de Insetos/metabolismo , Insetos/enzimologia , Tripsina/metabolismo , Animais , Sítios de Ligação , Catálise , Baratas/enzimologia , Besouros/enzimologia , Dípteros/enzimologia , Interações Hidrofóbicas e Hidrofílicas , Proteínas de Insetos/química , Proteínas de Insetos/isolamento & purificação , Cinética , Lepidópteros/enzimologia , Modelos Biológicos , Glycine max/metabolismo , Especificidade por Substrato , Tripsina/química , Tripsina/isolamento & purificação , Inibidores da Tripsina/metabolismoRESUMO
Many plant proteinase inhibitors have lysine at the P1 position, presumably to avoid hydrolysis by insect trypsins. Lepidopteran trypsins appear to have adapted to resist proteinase inhibitors through increased inhibitor hydrolysis and decreased binding to inhibitor hydrophilic reactive sites. Lepidopteran digestive trypsins prefer lysine at the P1 position and have substrate binding subsites more hydrophobic than trypsins from insects in other orders. All available sequences of sensitive and inhibitor-insensitive insect trypsins were aligned with porcine trypsin, for which interactions with Kunitz and Bowman-Birk inhibitor are known. After discounting conserved positions and positions not typical of sensitive or insensitive trypsins, the following residues were considered important to insect trypsin-PI interactions (chymotrypsin numbering): 60, 94, 97, 98, 99, 188, 190, 213, 215, 217, 219, 228. These residues support the Neighbor Joining analysis tree branches separating sensitive and insensitive trypsin sequences. Primary sequences interacting with PIs are around the active site, with some forming part of the S1 (188, 217, 219 and 228) or S4 (99, 215) pockets.
Assuntos
Proteínas de Insetos/antagonistas & inibidores , Proteínas de Insetos/genética , Insetos/enzimologia , Inibidores da Tripsina/genética , Tripsina/genética , Tripsina/metabolismo , Sequência de Aminoácidos , Aminoácidos/genética , Aminoácidos/metabolismo , Animais , Sítios de Ligação , Evolução Molecular , Proteínas de Insetos/metabolismo , Insetos/genética , Dados de Sequência Molecular , Filogenia , Proteínas de Plantas/genética , Proteínas de Plantas/metabolismo , Alinhamento de Sequência , Homologia de Sequência de Aminoácidos , Especificidade por Substrato , Inibidores da Tripsina/metabolismoRESUMO
A digestive trypsin from the American cockroach (Periplaneta americana, Dictyoptera) males was purified by a combination of anionic chromatographies in low and high pressure systems. The yield was 70% with a final specific activity of 2,000 units per mg protein (substrate: benzoyl-Arg-p-nitroanilide, BRpNA). Chemical modification with TLCK (k(obs)=3.3 M(-1) s(-1); stoichiometry 1:1) and PMSF (k(obs)=0.18 M(-1) s(-1); stoichiometry 1:1) confirmed that this peptidase is a trypsin. This enzyme has a molecular weight of 29 kDa (SDS-PAGE), a pI of 6.0 and a pH optimum of 8.9. Kinetic parameters using different colorimetric, fluorimetric and internally-quenched substrates indicated that P. americana trypsin prefers to hydrolyze synthetic substrates containing more than one amino acid residue and with an arginine residue at P1 position and a hydrophobic residue at P2. This enzyme presented a Km of 120 microM for BRpNA and is competitively inhibited by benzamidine (Ki=0.25 microM). Soybean trypsin inhibitor is a tight-binding inhibitor presenting a K(D) of 0.4 nM. Differences in substrate specificity and in the reactivity of the trypsin active site groups can be related to adaptation of insects to different hosts. P. americana trypsin is an excellent model for comparison as a basal group on evolutionary studies of insect trypsins.