RESUMO

This work presents a framework for evaluating hybrid nanoflowers using Burkholderia cepacia lipase. It was expanded on previous findings by testing lipase hybrid nanoflowers (hNF-lipase) formation over a wide range of pH values (5-9) and buffer concentrations (10-100 mM). The free enzyme activity was compared with that of hNF-lipase. The analysis, performed by molecular docking, described the effect of lipase interaction with copper ions. The morphological characterization of hNF-lipase was performed using scanning electron microscopy. Fourier Transform Infrared Spectroscopy performed the physical-chemical characterization. The results show that all hNF-lipase activity presented values higher than that of the free enzyme. Activity is higher at pH 7.4 and has the highest buffer concentration of 100 mM. Molecular docking analysis has been used to understand the effect of enzyme protonation on hNF-lipase formation and identify the main the main binding sites of the enzyme with copper ions. The hNF-lipase nanostructures show the shape of flowers in their micrographs from pH 6 to 8. The spectra of the nanoflowers present peaks typical of the amide regions I and II, current in lipase, and areas with P-O vibrations, confirming the presence of the phosphate group. Therefore, hNF-lipase is an efficient biocatalyst with increased catalytic activity, good nanostructure formation, and improved stability.

Assuntos

Cobre , Nanoestruturas , Estabilidade Enzimática , Cobre/química , Lipase/química , Simulação de Acoplamento Molecular , Nanoestruturas/química , Enzimas Imobilizadas/química , Espectroscopia de Infravermelho com Transformada de Fourier , Íons

RESUMO

Considerable amount of produced water discharged by the oil industry contributes to an environmental imbalance due to the presence of several components potentially harmful to the ecosystem. We investigated the factors influencing the adsorption capacity of Zinc Imidazolate Framework-8 (ZIF-8) in finite bath systems for crude oil removal from petroleum extraction in synthetic produced water. ZIF-8, experimentally obtained by solvothermal method, was characterized by XRD, FTIR, TGA, BET and its point of zero charge (pHpcz) was determined. Synthesized material showed high crystallinity, with surface area equal to 1558 m2 g-1 and thermal stability equivalent to 400 °C. Adsorption tests revealed, based on the Sips model, that the process takes place in a heterogeneous system. Additionally, intraparticle diffusion model exhibited multilinearity characteristics during adsorption process. Thermodynamic investigation demonstrated that adsorption process is spontaneous and exothermic, indicating a physisorption phenomenon. These properties enable the use of ZIF-8 in oil adsorption, which presented an adsorption capacity equal to 452.9 mg g-1. Adsorption mechanism was based on hydrophobic interactions, through apolar groups present on ZIF-8 structure and oil hydrocarbons, and electrostatic interactions, through the difference in charges between positive surface of adsorbent and negatively charged oil droplets.

Assuntos

Petróleo , Poluentes Químicos da Água , Ecossistema , Poluentes Químicos da Água/química , Água/química , Termodinâmica , Adsorção

RESUMO

The use of real space functions and molecular graphs has pushed some chemists to wonder: Are interactions between negatively charged oxygen atoms possible? In this contribution we analyze whether there is a real interaction between oxygen atoms in nitryl halide dimers (XNO2 )2 (X=F, Cl, Br and I) and in tetranitromethane and derivatives. Based on ab-initio and density functional theories (DFT) methods, we show these complexes are weakly stabilized. Energy decomposition analyses based on local molecular orbitals (LMOEDA) and interacting quantum atoms (IQA) reveal both dispersion and exchange play a crucial role in the stabilization of these complexes. Electron charge density and IQA analyses indicate that the oxygen atoms are connected by privileged exchange channels. In addition, electrostatic interactions between O and N atoms are also vital for the stabilization of the complexes. Finally, a reasonable explanation is given for the dynamic behavior of nitryl groups in tetranitromethane and derivatives.

RESUMO

Mesoporous carbon (MC) derived from cassava starch was used to remove Acid Blue 113 azo dye from aqueous solutions. The influence of temperature, pH, ionic strength, and the adsorbent dose was investigated in a set of batch experiments. Experimental data showed that Acid Blue 113 adsorption was higher in the acid pH range than in the alkaline one, that dye adsorption increases when the ionic strength and temperature increase, and that adsorption results presented a good correlation with the Langmuir isotherm model. The adsorption capacity of MC was 295 mg g-1, at pH = 7.0 and 298 K, respectively. Zeta potential (ζ) showed the compression of the diffuse double layer of adsorbent with an increase in temperature and ionic strength, promoting the decrease of electrostatic repulsion between the negatively charged surface of the carbon particles and the anionic dye. Thermodynamic results demonstrate that the adsorption process was spontaneous and endothermic. Moreover, for the first time, this work has demonstrated that the pH, temperature, and ionic strength of the aqueous medium are also able to change the surface charge of carbon-based adsorbents and surely influence the adsorption capacity. Finally, the regeneration of the adsorbent by the photo-Fenton reaction regenerated the adsorption capacity of the adsorbent without generating secondary pollution to the environment.

Assuntos

Carbono , Poluentes Químicos da Água , Adsorção , Temperatura , Compostos Azo , Concentração Osmolar , Água , Concentração de Íons de Hidrogênio , Amido , Cinética

RESUMO

Sulphur, not phosphorus, is the only known third-row element capable of experiencing an electrostatic gauche effect with fluorine. Some six-membered rings containing an endocyclic phosphorus atom and a ß-fluorine substituent that can interconvert to axial (gauche relative to phosphorus) and equatorial positions were then analysed. While phosphines do not establish an electrostatic attraction between fluorine and phosphorus, some oxidised forms exhibit surprising stability for the sterically disfavoured axial orientation. Because the nature of this behaviour was not obvious, since an intramolecular hydrogen bond can appear, a phosphonium derivative was further studied and its axial conformation was found to be highly stable. A preference for the gauche arrangement appears even for the acyclic and sterically hindered (2-fluoroethyl)triphenylphosphonium cation. On the other hand, (ethane-1,2-diyl)bis(phosphonium) cations are exclusively in anti conformation due to an (+/+)-electrostatic repulsion between the positively charged phosphonium groups.

Assuntos

Flúor , Flúor/química , Ligação de Hidrogênio , Conformação Molecular , Eletricidade Estática , Raios X

RESUMO

Studying the interactions of biopolymers like polysaccharides and proteins is quite important mainly due to the wide number of applications such as the stabilization and encapsulation of active compounds in complex systems. Complexation takes place when materials like proteins and polysaccharides are blended to promote the entrapment of active compounds. The interaction forces between the charged groups in the polymeric chains allow the miscibility of the components in the complex system. Understanding the interactions taking place between the polymers as well as between the wall material and the active compound is important when designing delivery systems. However, some features of the biopolymers like structure, functional groups, or electrical charge as well as extrinsic parameters like pH or ratios might affect the structure and the performance of the complex system when used in encapsulation applications. This work summarizes the recent progress of the polysaccharide/protein complexes for encapsulation and the influence of the pH on the structural modifications during the complexation process.

Assuntos

Polissacarídeos , Proteínas , Biopolímeros

RESUMO

BACKGROUND: Electrostatic interactions are one of the forces guiding the binding of molecules to proteins. The assessment of this interaction through computational approaches makes it possible to evaluate the energy of protein-drug complexes. OBJECTIVE: Our purpose here is to review some of the methods used to calculate the electrostatic energy of protein-drug complexes and explore the capacity of these approaches for the generation of new computational tools for drug discovery using the abstraction of scoring function space. METHODS: Here, we present an overview of the AutoDock4 semi-empirical scoring function used to calculate binding affinity for protein-drug complexes. We focus our attention on electrostatic interactions and how to explore recently published results to increase the predictive performance of the computational models to estimate the energetics of protein- drug interactions. Public data available at Binding MOAD, BindingDB, and PDBbind were used to review the predictive performance of different approaches to predict binding affinity. RESULTS: A comprehensive outline of the scoring function used to evaluate potential energy available in docking programs is presented. Recent developments of computational models to predict protein-drug energetics were able to create targeted-scoring functions to predict binding to these proteins. These targeted models outperform classical scoring functions and highlight the importance of electrostatic interactions in the definition of the binding. CONCLUSION: Here, we reviewed the development of scoring functions to predict binding affinity through the application of a semi-empirical free energy scoring function. Our studies show the superior predictive performance of machine learning models when compared with classical scoring functions and the importance of electrostatic interactions for binding affinity.

Assuntos

Preparações Farmacêuticas , Proteínas , Humanos , Ligantes , Aprendizado de Máquina , Eletricidade Estática

RESUMO

The COVID-19 pandemic has spread worldwide. However, as soon as the first vaccines-the only scientifically verified and efficient therapeutic option thus far-were released, mutations combined into variants of SARS-CoV-2 that are more transmissible and virulent emerged, raising doubts about their efficiency. This study aims to explain possible molecular mechanisms responsible for the increased transmissibility and the increased rate of hospitalizations related to the new variants. A combination of theoretical methods was employed. Constant-pH Monte Carlo simulations were carried out to quantify the stability of several spike trimeric structures at different conformational states and the free energy of interactions between the receptor-binding domain (RBD) and angiotensin-converting enzyme II (ACE2) for the most worrying variants. Electrostatic epitopes were mapped using the PROCEEDpKa method. These analyses showed that the increased virulence is more likely to be due to the improved stability to the S trimer in the opened state, in which the virus can interact with the cellular receptor, ACE2, rather than due to alterations in the complexation RBD-ACE2, since the difference observed in the free energy values was small (although more attractive in general). Conversely, the South African/Beta variant (B.1.351), compared with the SARS-CoV-2 wild type (wt), is much more stable in the opened state with one or two RBDs in the up position than in the closed state with three RBDs in the down position favoring the infection. Such results contribute to understanding the natural history of disease and indicate possible strategies for developing new therapeutic molecules and adjusting the vaccine doses for higher B-cell antibody production.

RESUMO

A new betacoronavirus named SARS-CoV-2 has emerged as a new threat to global health and economy. A promising target for both diagnosis and therapeutics treatments of the new disease named COVID-19 is the coronavirus (CoV) spike (S) glycoprotein. By constant-pH Monte Carlo simulations and the PROCEEDpKa method, we have mapped the electrostatic epitopes for four monoclonal antibodies and the angiotensin-converting enzyme 2 (ACE2) on both SARS-CoV-1 and the new SARS-CoV-2 S receptor binding domain (RBD) proteins. We also calculated free energy of interactions and shown that the S RBD proteins from both SARS viruses binds to ACE2 with similar affinities. However, the affinity between the S RBD protein from the new SARS-CoV-2 and ACE2 is higher than for any studied antibody previously found complexed with SARS-CoV-1. Based on physical chemical analysis and free energies estimates, we can shed some light on the involved molecular recognition processes, their clinical aspects, the implications for drug developments, and suggest structural modifications on the CR3022 antibody that would improve its binding affinities for SARS-CoV-2 and contribute to address the ongoing international health crisis.

Assuntos

Betacoronavirus/química , Peptidil Dipeptidase A/metabolismo , Receptores Virais/metabolismo , Coronavírus Relacionado à Síndrome Respiratória Aguda Grave/química , Glicoproteína da Espícula de Coronavírus/metabolismo , Enzima de Conversão de Angiotensina 2 , Anticorpos Monoclonais/imunologia , Anticorpos Monoclonais/metabolismo , Anticorpos Antivirais/imunologia , Anticorpos Antivirais/metabolismo , Betacoronavirus/imunologia , Simulação por Computador , Mapeamento de Epitopos , Humanos , Modelos Moleculares , Método de Monte Carlo , Peptidil Dipeptidase A/química , Ligação Proteica , Conformação Proteica , Domínios e Motivos de Interação entre Proteínas , Mapeamento de Interação de Proteínas , Receptores Virais/química , Coronavírus Relacionado à Síndrome Respiratória Aguda Grave/imunologia , SARS-CoV-2 , Glicoproteína da Espícula de Coronavírus/química , Glicoproteína da Espícula de Coronavírus/imunologia , Termodinâmica

RESUMO

Today, fluoride represents one of the most often found, and resilient, pollutants threatening the health of millions of people around the globe. The use of biosorbents is an interesting alternative technique for the removal of fluorine-ions. Chitosan is a natural biopolymer with surface groups capable of removing fluorine; however, their lack of mechanical stability restricts its application. In the present work, we proposed that such limitations can be overcame by forming a composite with zeolite (ZCC). A proper zeolite-to-chitosan ration must be kept to prevent a collapse of the material's capacity. Two ZCCs at ratios of 1:1 and 1:3 were formed and tested for the removal of fluoride from aqueous solution. The composites were characterized by Electron Microscopy, FT-IR, N2 physisorption, and potentiometric titration techniques. During fluoride adsorption studies, the effects of pH and temperature were analysed and thermodynamic parameters for adsorption were calculated. The results demonstrated that there is a chemical interaction between the zeolite and chitosan components leading to a superior adsorption performance than if there was a simple physical mixture of the precursors. Maximum adsorption capacities were reached using the composite material with the lowest chitosan content due to reduced constriction of the zeolite pores and a better dispersion of overall the adsorption sites. Both pH and temperature had a significant, and negative, impact on the adsorption; these effects were discussed. The present work represents an advance in the development of functional biocomposites for the removal of pollutants from aqueous solutions.

Assuntos

Quitosana , Poluentes Químicos da Água , Zeolitas , Adsorção , Fluoretos , Concentração de Íons de Hidrogênio , Cinética , Espectroscopia de Infravermelho com Transformada de Fourier

RESUMO

Computational analysis of protein-ligand interactions is of pivotal importance for drug design. Assessment of ligand binding energy allows us to have a glimpse of the potential of a small organic molecule as a ligand to the binding site of a protein target. Considering scoring functions available in docking programs such as AutoDock4, AutoDock Vina, and Molegro Virtual Docker, we could say that they all rely on equations that sum each type of protein-ligand interactions to model the binding affinity. Most of the scoring functions consider electrostatic interactions involving the protein and the ligand. In this chapter, we present the main physics concepts necessary to understand electrostatics interactions relevant to molecular recognition of a ligand by the binding pocket of a protein target. Moreover, we analyze the electrostatic potential energy for an ensemble of structures to highlight the main features related to the importance of this interaction for binding affinity.

Assuntos

Ligantes , Simulação de Acoplamento Molecular , Simulação de Dinâmica Molecular , Proteínas/química , Eletricidade Estática , Algoritmos , Sítios de Ligação , Desenho de Fármacos , Modelos Moleculares , Ligação Proteica

RESUMO

Nanocomposites of reduced graphene oxide (RGO) with ferromagnetic α-Fe2O3 nanoparticles have been prepared in-situ by thermal treatment. The structure and morphology of the hybrid material were studied by X-ray photoelectron spectroscopy, Raman, X-ray diffraction, and transmission electron microscopy. The results show a hybrid material highly modified with α-Fe2O3 nanoparticles distributed on the graphene surface. The adsorption kinetics show the presence of α-Fe2O3 nanoparticles on the RGO surface, and the amount of remaining functional groups dominated by ionization and dispersion. The adsorption kinetics of this adsorbent was characterized and found to fit the pseudo-second-order model. The α-Fe2O3 nanoparticles on RGO modify the electrostatic interaction of RGO layers and tetracycline, and adsorption properties decreased in the hybrid material. Adsorption isotherms fit with the Langmuir model very well, and the maximum capacity adsorption was 44.23 mg/g for RGO and 18.47 mg/g for the hybrid material. Magnetic characterization of the hybrid material shows ferromagnetic behavior due to the nanosize of α-Fe2O3 with a saturation magnetization, Ms = 7.15 Am²/kg, a remanence Mr = 2.29 Am²/kg, and a coercive field, Hc = 0.02 T.

RESUMO

Whey proteins are obtained from dairy industry waste. Studies involving the analysis of the bioactive compounds in whey show health benefits, as it is an excellent source of indispensable amino acids. Milk whey contains principally ß-lactoglobulin, α-lactoglobulin, bovine serum albumin, and lactoferrin, proteins with innumerable functional and technological properties. One application of these proteins in food is the formation of interpolymer complexes, along with other proteins or anionic polysaccharides. The formation of complexes occurs mainly through electrostatic interactions between a negatively charged biopolymer and a positively charged biopolymer. This formation is influenced by factors such as pH, ionic strength, and biopolymer ratio. Because they do not use high temperatures and chemical reagents and have additional nutritional and functional value, these complexes have been used as encapsulating agents for bioactive ingredients. Recent studies on their training and applications are addressed in this review to boost new research and applications in the food industry, thus increasing opportunities for utilizing whey proteins.

RESUMO

A hybrid simulation model (macro-molecular dynamics and Monte Carlo method) is proposed to reproduce neurosecretion and exocytosis. A theory has been developed for vesicular dynamics based on quasi-static electric interactions and a simple transition-state model for the vesicular fusion. Under the non-equilibrium electric conditions in an electrolytic fluid, it is considered that the motion of each synaptic vesicle is influenced by electrostatic forces exerted by the membranes of the synaptic bouton, other vesicles, the intracellular and intravesicular fluids, and external elements to the neuron. In addition, friction between each vesicle and its surrounding intracellular fluid is included in the theory, resulting in a drift type movement. To validate the vesicle equations of motion, a molecular dynamics method has been implemented, where the synaptic pool was replaced by a straight angle parallelepiped, the vesicles were represented by spheres and the fusion between each vesicle and the presynaptic membrane was simulated by a Monte Carlo type probabilistic change of state. Density profiles showing clusters of preferential activity as well as fusion distributions similar to the Poisson distributions associated with miniature end-plate potentials were obtained in the simulations.

Assuntos

Modelos Estatísticos , Neurossecreção , Eletricidade Estática , Vesículas Sinápticas , Animais , Exocitose/fisiologia , Método de Monte Carlo , Neurossecreção/fisiologia , Vesículas Sinápticas/fisiologia

RESUMO

Formation and characterization of droplet heteroaggregates were investigated by mixing two emulsions previously stabilized by proteins oppositely charged. Emulsions were composed of 5vol.% of sunflower oil and 95vol.% of sodium caseinate or lactoferrin aqueous dispersions. They were produced using ultrasound with fixed power (300W) and sonication time (6min). Different volume ratios (0-100%) of sodium caseinate-stabilized emulsion (droplet diameter around 1.75µm) to lactoferrin-stabilized emulsion (droplet diameter around 1.55µm) were mixed under conditions that both proteins showed opposite charges (pH7). Influence of ionic strength (0-400mM NaCl) on the heteroaggregates stability was also evaluated. Creaming stability, zeta potential, microstructure, mean particle diameter and rheological properties of the heteroaggregates were measured. These properties depended on the volume ratio (0-100%) of sodium caseinate to lactoferrin-stabilized emulsion (C:L) and the ionic strength. In the absence of salt, different zeta potential values were obtained, rheological properties (viscosity and elastic moduli) were improved and the largest heteroaggregates were formed at higher content of lactoferrin-stabilized emulsion (60-80%). The system containing 40 and 60vol.% of sodium caseinate and lactoferrin stabilized emulsion, respectively, presented good stability against phase separation besides showing enhanced rheological and size properties due to extensive droplets aggregation. Phase separation was observed only in the absence of sodium caseinate, demonstrating the higher susceptibility of lactoferrin to NaCl. The heteroaggregates produced may be useful functional agents for texture modification and controlled release since different rheological properties and sizes can be achieved depending on protein concentrations.

RESUMO

Polybia-MP1 (IDWKKLLDAAKQIL-NH2), extracted from the Brazilian wasp Polybia paulista, exhibits a broad-spectrum bactericidal activity without being hemolytic and cytotoxic. In the present study, we analyzed the surface properties of the peptide and its interaction with DPPC in Langmuir monolayers. Polybia-MP1 formed stable monolayers, with lateral areas and surface potential values suggesting a mostly α-helical structure oriented near perpendicular to the membrane plane. In DPPC-peptide mixed monolayers, MP1 co-crystallized with the lipid forming branched domains only when the subphase was pure water. On subphases with high salt concentrations or at acidic or basic conditions, the peptide formed less densely packed films and was excluded from the domains, indicating the presence of attractive electrostatic interactions between peptides, which allow them to get closer to each other and to interact with DPPC probably as a consequence of a particular peptide arrangement. The residues responsible of the peptide-peptide attraction are suggested to be the anionic aspartic acids and the cationic lysines, which form a salt bridge, leading to oriented interactions in the crystal and thereby to branched domains. For this peptide, the balance between total attractive and repulsive interactions may be finely tuned by the aqueous ionic strength and pH, and since this effect is related with lysines and aspartic acids, similar effects may also occur in other peptides containing these residues in their sequences.

Assuntos

1,2-Dipalmitoilfosfatidilcolina/química , Peptídeos Catiônicos Antimicrobianos/química , Membranas Artificiais , Venenos de Vespas/química , Estrutura Secundária de Proteína , Eletricidade Estática

RESUMO

Natural membranes are organized structures of neutral and charged molecules bearing dipole moments which generate local non-homogeneous electric fields. When subjected to such fields, the molecules experience net forces that can modify the lipid and protein organization, thus modulating cell activities and influencing (or even dominating) the biological functions. The energetics of electrostatic interactions in membranes is a long-range effect which can vary over distance within r-1 to r-3. In the case of a dipole interacting with a plane of dipoles, e.g. a protein interacting with a lipid domain, the interaction is stronger than two punctual dipoles and depends on the size of the domain. In this article, we review several contributions on how electrostatic interactions in the membrane plane can modulate the phase behavior, surface topography and mechanical properties in monolayers and bilayers.