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The intrinsically disordered C-terminal peptide region of severe acute respiratory syndrome coronavirus 2 nonstructural protein-1 (Nsp1-CT) inhibits host protein synthesis by blocking messenger RNA (mRNA) access to the 40S ribosome entrance tunnel. Aqueous copper(II) ions bind to the disordered peptide with micromolar affinity, creating a possible strategy to restore protein synthesis during host infection. Electron paramagnetic resonance (EPR) and tryptophan fluorescence measurements on a 10-residue model of the disordered protein region (Nsp1-CT10), combined with advanced quantum mechanics calculations, suggest that the peptide binds to copper(II) as a multidentate ligand. Two optimized computational models of the copper(II)-peptide complexes were derived: One corresponding to pH 6.5 and the other describing the complex at pH 7.5 to 8.5. Simulated EPR spectra based on the calculated model structures are in good agreement with experimental spectra.
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Cobre , Proteínas Intrínsecamente Desordenadas , SARS-CoV-2 , Proteínas no Estructurales Virales , Cobre/química , Cobre/metabolismo , Proteínas no Estructurales Virales/química , Proteínas no Estructurales Virales/metabolismo , Proteínas no Estructurales Virales/genética , SARS-CoV-2/metabolismo , SARS-CoV-2/química , Proteínas Intrínsecamente Desordenadas/química , Proteínas Intrínsecamente Desordenadas/metabolismo , Espectroscopía de Resonancia por Spin del Electrón , Humanos , Unión Proteica , Modelos Moleculares , COVID-19/virologíaRESUMEN
Smoothened (SMO) is an oncoprotein and signal transducer in the Hedgehog signaling pathway that regulates cellular differentiation and embryogenesis. As a member of the Frizzled (Class F) family of G protein-coupled receptors (GPCRs), SMO biochemically and functionally interacts with Gi family proteins. However, key molecular features of fully activated, G protein-coupled SMO remain elusive. We present the atomistic structure of activated human SMO complexed with the heterotrimeric Gi protein and two sterol ligands, equilibrated at 310 K in a full lipid bilayer at physiological salt concentration and pH. In contrast to previous experimental structures, our equilibrated SMO complex exhibits complete breaking of the pi-cation interaction between R4516.32 and W5357.55, a hallmark of Class F receptor activation. The Gi protein couples to SMO at seven strong anchor points similar to those in Class A GPCRs: intracellular loop 1, intracellular loop 2, transmembrane helix 6, and helix 8. On the path to full activation, we find that the extracellular cysteine-rich domain (CRD) undergoes a dramatic tilt, following a trajectory suggested by positions of the CRD in active and inactive experimental SMO structures. Strikingly, a sterol ligand bound to a shallow transmembrane domain (TMD) site in the initial structure migrates to a deep TMD pocket found exclusively in activator-bound SMO complexes. Thus, our results indicate that SMO interacts with Gi prior to full activation to break the molecular lock, form anchors with Gi subunits, tilt the CRD, and facilitate migration of a sterol ligand in the TMD to an activated position.
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Proteínas Hedgehog , Esteroles , Humanos , Esteroles/metabolismo , Ligandos , Modelos Moleculares , Proteínas Hedgehog/metabolismo , Receptores Acoplados a Proteínas G/metabolismo , Receptor Smoothened/metabolismoRESUMEN
Dipoles are ubiquitous, and their impacts on materials and interfaces affect many aspects of daily life. Despite their importance, dipoles remain underutilized, often because of insufficient knowledge about the structures producing them. As electrostatic analogues of magnets, electrets possess ordered electric dipoles. Here, we characterize the structural dynamics of bioinspired electret oligomers based on anthranilamide motifs. We report dynamics simulations, employing a force field that allows dynamic polarization, in a variety of solvents. The results show a linear increase in macrodipoles with oligomer length that strongly depends on solvent polarity and hydrogen-bonding (HB) propensity, as well as on the anthranilamide side chains. An increase in solvent polarity increases the dipole moments of the electret structures while decreasing the dipole effects on the moieties outside the solvation cavities. The former is due to enhancement of the Onsager reaction field and the latter to screening of the dipole-generated fields. Solvent dynamics hugely contributes to the fluctuations and magnitude of the electret dipoles. HB with the solvent weakens electret macrodipoles without breaking the intramolecular HB that maintains their extended conformation. This study provides design principles for developing a new class of organic materials with controllable electronic properties. An animated version of the TOC graphic showing a sequence of the MD trajectories of short and long molecular electrets in three solvents with different polarities is available in the HTML version of this paper.
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The glucagon-like peptide-1 receptor (GLP-1R) is a key regulator of blood glucose and a prime target for the treatment of type II diabetes and obesity with multiple public drugs. Here we present a comprehensive computational analysis of the interactions of the activated GLP-1R-Gs signaling complex with a G protein biased agonist, Exendin P5 (ExP5), which possesses a unique N-terminal sequence responsible for the signal bias. Using a refined all-atom model of the ExP5-GLP-1R-Gs complex in molecular dynamics (MD) simulations, we propose a novel mechanism of conformation transduction in which the unique interaction network of ExP5 N-terminus propagates the binding signal across an array of conserved residues at the transmembrane domain to enhance Gs protein coupling at the cytoplasmic end of the receptor. Our simulations reveal previously unobserved interactions important for activation by ExP5 toward GDP-GTP signaling, providing new insights into the mechanism of class B G protein-coupled receptor (GPCR) signaling. These findings offer a framework for the structure-based design of more effective therapeutics.
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Diabetes Mellitus Tipo 2 , Receptor del Péptido 1 Similar al Glucagón , Humanos , Transducción de Señal , Glucemia , CitoplasmaRESUMEN
Biopanning refers to the processes of screening peptides with a high affinity to a target material. Microfluidic biopanning has advantages compared to conventional biopanning which requires large amounts of the target material and involves inefficient multiple pipetting steps to remove nonspecific or low-affinity peptides. Here, we fabricate a microfluidic biopanning system to identify a new gold-binding peptide (GBP). A polydimethylsiloxane microfluidic device is fabricated and bonded to a glass slide with a gold pattern that is deposited by electron-beam evaporation. The microfluidic biopanning system can provide high adjustability in the washing step during the biopanning process because the liquid flow rate and the resulting shear stress can be precisely controlled. The surface plasmon resonance analysis shows that the binding affinity of the identified GBP is comparable to previously reported GBPs. Moreover, molecular dynamics simulations are performed to understand its binding affinity against the gold surface in detail. Theoretical calculations suggest that the association and dissociation rates of the GBPs depend on their sequence-dependent conformations and interactions with the gold surface. These findings provide insight into designing efficient biopanning tools and peptides with a high affinity for various target materials.
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Oro/metabolismo , Péptidos/metabolismo , Dimetilpolisiloxanos/química , Dispositivos Laboratorio en un Chip , Microfluídica/instrumentación , Microfluídica/métodos , Simulación de Dinámica Molecular , Péptidos/química , Unión Proteica , Conformación ProteicaRESUMEN
The extracellular lipid matrix in the stratum corneum (SC) plays a critical role in skin barrier functionality, comprising three primary components: ceramides, cholesterol, and free fatty acids. The diverse ceramides, differentiated by molecular structures such as hydroxylations and varying chain lengths, are essential for the lipid matrix's structural integrity. Recently, a new subclass of ceramide, 1-O-acylceramide NP (CerENP), has been identified; however, its precise role in the lipid matrix of the SC is still elusive. Herein, we investigate the role of CerENP on the structure and permeability of the SC using molecular dynamics simulations. Our findings indicate that CerENP contributes to a compact lipid matrix in the lateral dimension of our SC model with a repeat distance of about 13 nm. Additionally, ethanol permeability assessments show that CerENP effectively reduces molecular penetration through the lipid matrix. This study provides an insight into the role of a new subclass of ceramide in the SC, enhancing our understanding of skin structure and the mechanisms behind barrier dysfunction in skin diseases.
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Ceramidas , Simulación de Dinámica Molecular , Ceramidas/química , Epidermis/metabolismo , Epidermis/química , Permeabilidad , Humanos , Piel/metabolismo , Piel/química , Lípidos/química , Etanol/químicaRESUMEN
Pauling and Corey expected that a racemic mixture would result in a rippled ß-sheet, however, it has been known from experiments that the racemic mixtures of triphenylalanine lead to a herringbone structure. Because of the theoretical limitations concerning crystal structures such as rippled ß-sheet, it is inevitable to understand how the interplay of the amino acids prefers a specific structural motif. In this paper we use molecular dynamics to understand the sequence- and enantiomer-dependent structures by comparisons between rippled ß-sheet and pleated ß-sheet, solvated and anhydrous rippled ß-sheet, and rippled ß-sheet and the herringbone structure, based on thermodynamics and structures at the atomic level. The tripeptides select the favored structure that can be stabilized through aromatic or hydrogen bonding interactions between tripeptides. Furthermore, the solubility is determined by the environment of space that is created around the side chains. Our findings provide comprehensive insight into the crystallized fibril motif of the polypeptide.
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Constructing an artificial solid electrolyte interphase (SEI) on lithium metal electrodes is a promising approach to address the rampant growth of dangerous lithium morphologies (dendritic and dead Li0) and low Coulombic efficiency that plague development of lithium metal batteries, but how Li+ transport behavior in the SEI is coupled with mechanical properties remains unknown. We demonstrate here a facile and scalable solution-processed approach to form a Li3N-rich SEI with a phase-pure crystalline structure that minimizes the diffusion energy barrier of Li+ across the SEI. Compared with a polycrystalline Li3N SEI obtained from conventional practice, the phase-pure/single crystalline Li3N-rich SEI constitutes an interphase of high mechanical strength and low Li+ diffusion barrier. We elucidate the correlation among Li+ transference number, diffusion behavior, concentration gradient, and the stability of the lithium metal electrode by integrating phase field simulations with experiments. We demonstrate improved reversibility and charge/discharge cycling behaviors for both symmetric cells and full lithium-metal batteries constructed with this Li3N-rich SEI. These studies may cast new insight into the design and engineering of an ideal artificial SEI for stable and high-performance lithium metal batteries.
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In order to investigate Li2S as a potential protective coating for lithium anode batteries using superionic electrolytes, we need to describe reactions and transport for systems at scales of >10,000 atoms for time scales beyond nanoseconds, which is most impractical for quantum mechanics (QM) calculations. To overcome this issue, here, we first report the development of the reactive analytical force field (ReaxFF) based on density functional theory (DFT) calculations on model systems at the PBE0/TZVP and M062X/TZVP levels. Then, we carry out reactive molecular dynamics simulations (RMD) for up to 20 ns to investigate the diffusion mechanisms in bulk Li2S as a function of vacancy density, determining the activation barrier for diffusion and conductivity. We show that RMD predictions for diffusion and conductivity are comparable to experiments, while results on model systems are consistent with and validated by short (10-100 ps) ab initio molecular dynamics (AIMD). This new ReaxFF for Li2S systems enables practical RMD on spatial scales of 10-100 nm (10,000 to 10 million atoms) for the time scales of 20 ns required to investigate predictively the interfaces between electrodes and electrolytes, electrodes and coatings, and coatings and electrolytes during the charging and discharging processes.
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Chronic exposure to stress or unwanted stimuli has been known to activate kappa opioid receptor/dynorphin (KOR/DYN) systems, which could induce depressive states and develop into some psychiatric disorders. Here, we report the first discovery of pyrazoloisoquinoline-based novel KOR ß-arrestin inverse agonists through synthesis, structure-activity relationships, optimization, and the biological evaluations of µ/κ/δ opioid receptor activities with cAMP and ß-arrestin recruitment assays. The optimized compound 7q shows potent and selective ß-arrestin inverse agonism at KOR with an EC50 value of 9.33 nM in contrast to lower activities at DOR and no activity at MOR. Moreover, we use molecular dynamics simulations to predict the binding mode of the inverse agonist and propose a mechanism for the inverse agonism. We find that the transmembrane helix 6 position of the activated state is different for the OR subtypes, leading to significantly different interactions between the receptor and ß-arrestin.
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Agonismo Inverso de Drogas , Receptores Opioides kappa , Humanos , Receptores Opioides kappa/metabolismo , beta-Arrestinas/metabolismo , Dinorfinas/metabolismo , Relación Estructura-Actividad , Receptores Opioides mu/metabolismoRESUMEN
Metabotropic γ-aminobutyric acid receptor (GABABR), a class C G protein-coupled receptor (GPCR) heterodimer, plays a crucial role in the central nervous system. Cryo-electron microscopy studies revealed a drastic conformational change upon activation and a unique G protein (GP) binding mode. However, little is known about the mechanism for GP coupling and activation for class C GPCRs. Here, we use molecular metadynamics computations to predict the mechanism by which the inactive GP induces conformational changes in the GABABR transmembrane domain (TMD) to form an intermediate pre-activated state. We find that the inactive GP first interacts with TM3, which further leads to the TMD rearrangement and deeper insertion of the α5 helix that causes the Gα subunit to open, releasing GDP, and forming the experimentally observed activated structure. This mechanism provides fresh insights into the mechanistic details of class C GPCRs activation expected to be useful for designing selective agonists and antagonists.
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Proteínas de Unión al GTP , Ácido gamma-Aminobutírico , Membrana Celular/metabolismo , Microscopía por Crioelectrón , Proteínas de Unión al GTP/metabolismo , Unión Proteica , Dominios Proteicos , Receptores de GABA-B/genética , Receptores de GABA-B/metabolismo , Ácido gamma-Aminobutírico/metabolismoRESUMEN
Bitter taste receptors (TAS2Rs) function in taste perception, but are also expressed in many extraoral tissues, presenting attractive therapeutic targets. TAS2R5s expressed on human airway smooth muscle cells can induce bronchodilation for treating asthma and other obstructive diseases. But TAS2R5s display low agonist affinity and the lack of a 3D structure has hindered efforts to design more active ligands. We report the structure of the activated TAS2R5 coupled to the Gi protein and bound to each of 19 agonists, using computational approaches. These agonists bind to two polar residues in TM3 that are unique for TAS2R5 among 25 TAS2R subtypes. Our predicted results correlate well with experimental results of agonist-receptor signaling coefficients, providing validation of the predicted structure. These results provide highly specific data on how agonists activate TAS2R5, how modifications of ligand structure alter receptor activation, and a guide to structure-based drug design.
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Subunidades alfa de la Proteína de Unión al GTP Gi-Go/química , Receptores Acoplados a Proteínas G/agonistas , Sitios de Unión , Subunidades alfa de la Proteína de Unión al GTP Gi-Go/metabolismo , Humanos , Simulación de Dinámica Molecular , Isoformas de Proteínas/agonistas , Isoformas de Proteínas/química , Isoformas de Proteínas/metabolismo , Estructura Terciaria de Proteína , Receptores Acoplados a Proteínas G/química , Receptores Acoplados a Proteínas G/metabolismo , TermodinámicaRESUMEN
Bitter taste is sensed by bitter taste receptors (TAS2Rs) that belong to the G protein-coupled receptor (GPCR) superfamily. In addition to bitter taste perception, TAS2Rs have been reported recently to be expressed in many extraoral tissues and are now known to be involved in health and disease. Despite important roles of TAS2Rs in biological functions and diseases, no crystal structure is available to help understand the signal transduction mechanism or to help develop selective ligands as new therapeutic targets. We report here the three-dimensional structure of the fully activated TAS2R4 human bitter taste receptor predicted using the GEnSeMBLE complete sampling method. This TAS2R4 structure is coupled to the gustducin G protein and to each of several agonists. We find that the G protein couples to TAS2R4 by forming strong salt bridges to each of the three intracellular loops, orienting the activated Gα5 helix of the Gα subunit to interact extensively with the cytoplasmic region of the activated receptor. We find that the TAS2Rs exhibit unique motifs distinct from typical Class A GPCRs, leading to a distinct activation mechanism and a less stable inactive state. This fully activated bitter taste receptor complex structure provides insight into the signal transduction mechanism and into ligand binding to TAS2Rs.
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Heterogeneous tissue models require the assembly and co-culture of multiple types of cells. Our recent work demonstrated taste signal transmission from gustatory cells to neurons by grafting single-stranded DNA into the cell membrane to construct multicellular assemblies. However, the weak DNA linkage and low grafting density allowed the formation of large gustatory cell self-aggregates that cannot communicate with neurons efficiently. This article presents the construction of artificial taste buds exhibiting active intercellular taste signal transmission through the hybridization of gustatory-neuronal multicellular interfaces using bioorthogonal click chemistry. Hybrid cell clusters were formed by the self-assembly of neonatal gustatory cells displaying tetrazine with a precultured embryonic hippocampal neuronal network displaying trans-cyclooctene. A bitter taste signal transduction was provoked in gustatory cells using denatonium benzoate and transmitted to neurons as monitored by intracellular calcium ion sensing. In the multicellular hybrids, the average number of signal transmissions was five to six peaks per cell, and the signal transmission lasted for â¼5 min with a signal-to-signal gap time of 10-40 s. The frequent and extended intercellular signal transmission suggests that the cell surface modification by the bioorthogonal click chemistry is a promising approach to fabricating functional multicellular hybrid clusters potentially useful for cell-based biosensors, toxicity assays, and tissue regeneration.
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Papilas Gustativas , Técnicas de Cocultivo , Neuronas , Transducción de Señal , GustoRESUMEN
Protein encapsulation into nanocarriers has been extensively studied to improve the efficacy and stability of therapeutic proteins. However, the chemical modification of proteins or new synthetic carrier materials are essential to achieve a high encapsulation efficiency and structural stability of proteins, which hinders their clinical applications. New strategies to physically incorporate proteins into nanocarriers feasible for clinical uses are required to overcome the current limitation. Here we report the spontaneous protein-induced reorganization of 'pre-formed' unilamellar lipid vesicles to efficiently incorporate proteins within multilamellar protein-lipid hybrid vesicles without chemical modification. Epidermal growth factor (EGF) binds to the surface of cationic unilamellar lipid vesicles and induces layer-by-layer self-assembly of the vesicles. The protein is spontaneously entrapped in the interstitial layers of a multilamellar structure with extremely high loading efficiency, ~99%, through polyionic interactions as predicted by molecular dynamics simulation. The loaded protein exhibits much higher structural, chemical, and biological stability compared to free protein. The method is also successfully applied to several other proteins. This work provides a promising method for the highly efficient encapsulation of therapeutic proteins into multilamellar lipid vesicles without the use of specialized instruments, high energy, coupling agents, or organic solvents.
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Liposomas , Liposomas Unilamelares , Cationes , Lípidos , SolventesRESUMEN
Quantum dots (QDs) can serve as an attractive Förster resonance energy transfer (FRET) donor for DNA assay due to their excellent optical properties. However, the specificity and sensitivity of QD-based FRET analysis are prominently reduced by nonspecific DNA adsorption and poor colloidal stability during DNA hybridization, which hinders the practical applications of QDs as a biosensing platform. Here, we report subnanomolar FRET assay of DNA through the stabilization of DNA/QD interface using DNA-functionalized QDs with phosphorothioated single-stranded DNA (pt-ssDNA) as a multivalent ligand in an aqueous solution. In situ DNA functionalization was achieved during the aqueous synthesis of CdTe/CdS QDs, resulting in the maximum photoluminescence quantum yields of 76.9% at an emission wavelength of 732 nm. Conventional monothiolated ssDNA-capped QDs exhibited particle aggregation and photoluminescence (PL) quenching during DNA hybridization at 70 °C due to the dissociation of surface ligands. Such colloidal instability induced the nonspecific adsorption of DNA, resulting in false-positive signal and decreased sensitivity with the limit of detection (LOD) of 16.1 nM. In contrast, the pt-ssDNA-functionalized QDs maintained their colloidal stability and PL properties at elevated temperatures. The LOD of the pt-ssDNA-functionalized QDs was >30 times lower (0.47 nM) while maintaining the high specificity to a target sequence because the strong multivalent binding of pt-ssDNA to the surface of QDs prevents the detachment of pt-ssDNA and nonspecific adsorption of DNA. The study suggests that the ligand design to stabilize the surface of QDs in an aqueous milieu is critically important for the high performance of QDs for specific DNA assay.
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ADN de Cadena Simple/análisis , ADN de Cadena Simple/química , Transferencia Resonante de Energía de Fluorescencia , Puntos Cuánticos/química , ColoidesRESUMEN
Natural photosystems (PSs) have received much attention as a biological solar energy harvester because of their high quantum efficiency for energy transfer. However, the PSs hybridized with solid electrodes exhibit low light-harvesting efficiencies because of poor interface properties and random orientations of PSs, all of which interfere with efficient charge extraction and transfer. Herein, we report the linker-free, oriented self-assembly of natural PSs with nitrogen-doped carbon nanotubes (NCNTs) via electrostatic interaction. Protonated nitrogen-doped sites on the NCNTs facilitate spontaneous immobilization of the negatively charged stroma side of PSs, which provides a favorable orientation for electron transfer without electrically insulating polymer linkers. The resulting PS/NCNT hybrids exhibit a photocurrent density of 1.25 ± 0.08 µA cm-2, which is much higher than that of PS/CNT hybrids stabilized with polyethylenimine (0.60 ± 0.01 µA cm-2) and sodium dodecyl sulfate (0.14 ± 0.01 µA cm-2), respectively. This work emphasizes the importance of the linker-free assembly of PSs into well-oriented hybrid structures to construct an efficient light-harvesting electrode.
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Tumor-targeted delivery of anticancer agents using nanocarriers has been explored to increase the therapeutic index of cancer chemotherapy. However, only a few nanocarriers are clinically available because the physiological complexity often compromises their ability to target, penetrate, and control the release of drugs. Here, we report a method which dramatically increases in vivo therapeutic drug efficacy levels through the photodynamic degradation of tumor-targeted nanocarriers. Folate-decorated poly(ethylene glycol)-polythioketal micelles are prepared to encapsulate paclitaxel and porphyrins. Photo-excitation generates reactive oxygen species within the micelles to cleave the polythioketal backbone efficiently and facilitate drug release only at the illuminated tumor site. Intravenous injection of a murine xenograft model with a low dose of paclitaxel within the micelles, one-milligram drug per kg (mouse), corresponding to an amount less than that of Taxol by one order of magnitude, induces dramatic tumor regression without any acute systemic inflammation responses or organ toxicity under low-power irradiation (55â¯mWâ¯cm-2) at 650â¯nm.
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Antineoplásicos Fitogénicos/administración & dosificación , Preparaciones de Acción Retardada/metabolismo , Micelas , Neoplasias/tratamiento farmacológico , Paclitaxel/administración & dosificación , Porfirinas/administración & dosificación , Especies Reactivas de Oxígeno/metabolismo , Animales , Antineoplásicos Fitogénicos/farmacocinética , Antineoplásicos Fitogénicos/uso terapéutico , Sistemas de Liberación de Medicamentos/métodos , Ácido Fólico/metabolismo , Células HeLa , Humanos , Masculino , Ratones Endogámicos BALB C , Ratones Desnudos , Neoplasias/metabolismo , Paclitaxel/farmacocinética , Paclitaxel/uso terapéutico , Fotoquimioterapia/métodos , Polietilenglicoles/metabolismo , Porfirinas/farmacocinética , Porfirinas/uso terapéuticoRESUMEN
Despite the excellent biocompatibility and antifouling effect of poly(ethylene glycol) (PEG), the high steric hindrance, limited chemical functionality, and low ligand multivalency of PEGylated nanocarriers often lead to inefficient cell targeting and intracellular trafficking. Hence, a new structure of hydrophilic corona allowing a higher ligand density without loss of excellent biocompatibility is highly desirable. Here we introduce tumor-targeted polyglycerolated (PGylated) nanocarriers that dramatically enhance the in vivo therapeutic efficacy of incorporated paclitaxel simply by increasing the surface density of hydrophobic tumor-targeting ligands. Linear polyglycerol-poly (ε-caprolactone) block copolymer (PG-b-PCL) is used to prepare PGylated lipiodol nanoemulsions, where PG serves as a corona conjugated with a large number of folic acid (FA) for efficient tumor targeting. Unlike FA-PEGylated nanoemulsions, FA-PGylated nanoemulsions can display a larger number of FA without structural destabilization. This property enables excellent anti-cancer activities and effective tumor regression in a cervical cancer xenograft murine model at a cumulative drug dose of â¼5 mg kg-1, which is about four fold smaller than that of commercial Taxol formulation. This study highlights the importance of surface chemistry of nanocarriers that enable multivalent ligand functionalization and high tolerance to the conjugation of hydrophobic ligands, which make PG as a very effective hydrophilic corona for in vivo drug delivery.
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Portadores de Fármacos/química , Glicerol/química , Nanopartículas/química , Paclitaxel/uso terapéutico , Polímeros/química , Animales , Femenino , Fluorescencia , Células HeLa , Humanos , Ligandos , Ratones Endogámicos BALB C , Ratones Desnudos , Simulación de Dinámica Molecular , Poliésteres/químicaRESUMEN
Immobilization of nanometer-sized metal catalysts into porous substrates can stabilize the catalysts and allow their recycled uses, while immobilization often sacrifices the active surface of catalysts and degenerates the local microenvironments, resulting in the reduction of the catalytic activity. To maintain a high activity of immobilized nanocatalysts, it is critically important to design an interface that minimizes the contact area and favors reaction chemistry. Here we report on the application of mussel-inspired adhesion chemistry to the formation of catalytic metal nanocrystal-polydopamine hybrid materials that exhibit a high catalytic efficiency during recycled uses. Electrospun polymer nanofibers are used as a template for in situ formation and immobilization of gold nanoparticles via polydopamine-induced reduction of ionic precursors. The prepared hybrid nanostructures exhibit a recyclable catalytic activity for the reduction of 4-nitrophenol with a turnover frequency of 3.2-5.1 µmol g(-1) min(-1). Repeated uses of the hybrid nanostructures do not significantly alter their morphology, indicating the excellent structural stability of the hybrid nanostructures. We expect that the polydopamine chemistry combined with the on-surface synthesis of catalytic nanocrystals is a promising route to the immobilization of various colloidal nanosized catalysts on supporting substrates for long-term catalysis without the physical instability problem.