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Background: Candida is one of the common pathogens in nosocomial infections. Culture is the gold standard for diagnosing candidemia. Candida albicans is identified via the germ tube test, which uses serum as the culture medium, which is costly and time-consuming. This study was conducted to evaluate and compare a relatively simple, fast, and reliable method for the detection of Candida albicans. Methods: We conducted this randomized case study at Taipei City Hospital (TCH) from January 2023 to August 2023, with a total of 30 specimen culture reports collected and confirmed to be cases of Candida albicans infection. A germ tube test was performed in a 37°C water bath using serum, plasma, and safe plasma products (Fresh Frozen Plasma, FFP). Further, the same procedures were repeated with the addition of 22% bovine serum albumin (BSA) to the identification/culture. Results: By adding BSA, more than 50% of the budding phenomenon was observed in 40 minutes, which shortened the diagnosis time compared with the traditional method (2-3 hours). Using BSA can shorten the identification time for early clinical medication and improve the quality of medical care. Conclusion: Using safer plasma products for germ tube test of candidiasis not only reduced the risk of infection for medical technicians but could also replace the serum used in traditional methods to increase convenience and save time. This study proposed BSA as a germ tube induction medium enhancer, which reduced the culture time, thereby enabling quicker diagnosis of C. albicans infections.
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Recently, we have described the first supermolecular nanoentities of vitamin B12 derivative, viz. monocyano form of heptabutyl cobyrinate, unique nanoparticles with strong noncovalent intermolecular interactions, emerging optical and catalytic properties. Their nearest analogue, heptamethyl cobyrinate (ACCby), exhibits bioactivity. Here, we demonstrate the first example of the formation of nanoparticles of this nucleotide-free analogue of vitamin B12 in protein nanocarriers and neuroprotective activity in vivo of the own nanoform of the drug. The preparation and characterization of nanocarriers based on bovine serum albumin (BSA) loaded with vitamin B12 (viz. cyano- and aquacobalamins) and ACCby were performed. Nucleotide-free analogue of vitamin B12 is tightly retained by the protein structure and exists in an incorporated state in the form of nanoparticles. The effect of encapsulated drugs on the character and severity of primary generalized seizures in rats induced by the pharmacotoxicant thiosemicarbazide was studied. Cyanocobalamin and ACCby exhibited a neuroprotective effect. The best influence of the encapsulation on the effectiveness of the drugs was achieved in the case of AСCby, whose bioavailability as a neuroprotector did not change upon introduction in BSA particles, i.e., 33â¯% of surviving animals were observed upon ACCby administration in free form and in encapsulated state. No surviving rats were observed without the administration of drugs. Thus, BSA nanocarriers loaded by nanoparticles of nucleotide-free analogues of vitamin B12, including hydrophobic ones, can be recommended for neuroprotection and targeted delivery.
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Portadores de Fármacos , Nanopartículas , Fármacos Neuroprotectores , Albúmina Sérica Bovina , Vitamina B 12 , Animales , Vitamina B 12/análogos & derivados , Vitamina B 12/química , Vitamina B 12/farmacología , Albúmina Sérica Bovina/química , Nanopartículas/química , Fármacos Neuroprotectores/química , Fármacos Neuroprotectores/farmacología , Portadores de Fármacos/química , Ratas , Masculino , Ratas Wistar , Bovinos , Convulsiones/tratamiento farmacológico , Convulsiones/prevención & controlRESUMEN
By using crawfish shells as the precursor and hydrothermal synthesis, Bovine serum albumin doped carbon dots (BSA@CDs) were prepared without excessive chemical reagents. The relationship between the fluorescence properties of different BSA@CDs and BSA amount was investigated by variouscharacterization techniques. When the amount of BSA added was 30 %, the prepared BSA@CDs' quantum yield (QY) reached 25.01 %, which was the highest. Inner Filter Effect (IFE) suggested that Cr (VI) can selectively quench the fluorescence of BSA@CDs. Cr (VI) can be reduced to Cr (III) by Hydroquinone (HQ), thus recovering the fluorescence. Accordingly, using BSA@CDs as a probe, a "turn-on" fluorescence sensor applied in HQ determination was constructed. The linear range was 10-200 µmol/L and limit of detection (LOD) was 0.18 µmol/L. Further, it has been employed to the determination of HQ in both crawfish tail meat and aquaculture water with good performance.
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Understanding the mass transfer behaviors in hollow fiber membrane module of artificial liver is important for improving toxin removal efficiency. A three-dimensional numerical model was established to study the mass transfer of small molecule bilirubin and macromolecule bovine serum albumin (BSA) in the hollow fiber membrane module. Effects of tube-side flow rate, shell-side flow rate, and hollow fiber length on the mass transfer of bilirubin and BSA were discussed. The simulation results showed that the clearance of bilirubin was significantly affected by both convective and diffusive solute transport, while the clearance of macromolecule BSA was dominated by convective solute transport. The clearance rates of bilirubin and BSA increasd with the increase of tube-side flow rate and hollow fiber length. With the increase of shell-side flow rate, the clearance rate of bilirubin first rose rapidly, then slowly rose to an asymptotic value, while the clearance rate of BSA gradually decreased. The results can provide help for designing structures of hollow fiber membrane module and operation parameters of clinical treatment.
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Bilirrubina , Hígado Artificial , Membranas Artificiales , Albúmina Sérica Bovina , Albúmina Sérica Bovina/química , Bilirrubina/metabolismo , Animales , Bovinos , HumanosRESUMEN
Orally administered amoxicillin is recommended as the first-line treatment of acute bacterial rhinosinusitis (ABR) and given in a high-dose regimen. However, the risk of various systemic adverse reactions and low oral bioavailability are unbearable, increasing the threat of antibiotic resistance. Therefore, nasal delivery of amoxicillin can be a potential approach for effectively treating ABR locally, as well as overcoming those drawbacks. In a way to guarantee the effectiveness for local therapy in nasal cavity, the permeation and retention properties are of significant importance considerations. Accordingly, the present work aimed to investigate the characteristics with respect to the nasal applicability of the in situ gelling amoxicillin trihydrate (AMT) and further evaluate its permeability and retention properties through human nasal mucosa. The lyophilized formulations were characterized utilizing the Differential Scanning Calorimetry (DSC) and X-ray Powder Diffraction (XRPD), and also evaluated for its polarity, reconstitution time, droplet size distribution, mucoadhesive properties, and ex vivo permeability and retention studies. The results confirmed that the in situ gelling AMT formulations possess adequate mucoadhesive behavior, especially the formulation containing 0.3 % of gellan gum. Substantially, the in situ gelling AMT formulations were able to retain the drug on the surface of nasal mucosa instead of permeating across the membrane; thus, suitable for treating nasal infections locally. Altogether, the in situ gelling systems demonstrates promising abilities as a delivery platform to enhance local application of AMT within the nasal cavity.
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Bovine serum albumin (BSA) is widely used in tissue engineering and pharmaceutical research. It is readily available as a byproduct of the cattle industry, collected from blood. In this study, we conducted a physicochemical investigation of the phase separation in a mixture of Triton X-100 (TX-100) and BSA, influenced by various polyols, using the well-established cloud point (CP) determination method. The addition of polyols resulted in a significant reduction in CP values for the TX-100â¯+â¯BSA mixture. For the system under investigation with polyols, the CP values followed the order: [Formula: see text] Under identical conditions, the system exhibited maximum solubility in the xylose solution and minimum solubility in the maltose solution. At lower polyol content, negative values of standard enthalpy (∆Hc0) and standard entropy (∆Sc0) changes were observed, suggesting that electrostatic forces dominate as the driving force for clouding. At highest employed polyol concentration in some case, positive values for ∆Hc0 and ∆Sc0 were achieved, which indicated that hydrophobic interactions likely dominate the phase partitioning of the amphiphile and protein mixture. Additionally, entropy-enthalpy compensation parameters were calculated and analyzed with a rational approach. Molecular docking analysis further demonstrated the presence of hydrogen bonds and hydrophobic interactions between TX-100 and BSA.
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Nano bimetallic oxides as nanoproteases have the great advantages in the heterogeneous hydrolysis of proteins. Here, we report that bimetallic delafossite CuFeO2 submicron particles (CuFeO2 SMPs) display a high protease activity towards selective cleavage of peptide bond involving hydrophobic residue at 25 centidegree. CuFeO2 SMPs have excellent regeneration performance with high structural stability. The strong Lewis acidity of Fe(III) and the strong nucleophilicity of Cu(I) bound hydroxyl groups are both necessary for the high protease activity of CuFeO2 SMPs. Low-valent metal ion has a great advantage in that low-valent Cu(I) bound hydroxyl has strong nucleophilicity, resulting in promotion of protein hydrolysis via high-efficient bimetallic catalysis. This study provides evidence that the protease activity of CuFeO2 SMPs depends on metal ion-bound hydroxyls on their surface. Our findings highlight that the valence of metal ions in artificial protease and their surface hydroxyls are two important factors that determine their catalytic efficiency.
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Antiglomerular basement membrane (GBM) disease has a poor prognosis. The rapid detection of serum anti-GBM antibody using an enzyme immunoassay, which has a high sensitivity and specificity, leads to an early diagnosis and improved prognosis. We report a case of acute kidney injury with false-positive anti-GBM antibody. A man in his early fifties underwent aortic arch replacement using bovine serum albumin (BSA)-containing surgical adhesion. After intravenous administration of vancomycin for a fever, he developed acute kidney injury without an abnormal urinalysis, and his anti-GBM antibody titer (fluorescence enzyme immunoassay [FEIA]) was 70.4 IU/mL. A kidney biopsy showed acute tubular injury and minor glomerular abnormalities without immunoglobulin G deposits, suggesting no evidence of anti-GBM glomerulonephritis. Consistent with the false-positive anti-GBM antibody test results, anti-GBM antibody determined using a chemiluminescent enzyme immunoassay was negative. A serum sample showed crossbinding to the FEIA plate from which the GBM antigen was removed. This finding indicated a nonspecific reaction to BSA, which contains a coating solution for the FEIA plate. This reaction was likely caused by anti-BSA antibody produced using BSA-containing surgical adhesion. Our findings suggest emerging challenges in diagnosing anti-GBM disease. Nephrologists must remain vigilant regarding false-positive anti-GBM antibody test results, particularly in cases evaluated with immunoassays that contain BSA.
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Breast cancer is a prominent cause of death among women and is distinguished by a high occurrence of metastasis. From this perspective, apart from conventional therapies, several alternative approaches have been researched and explored in recent years, including the utilization of nano-albumin and statin medications like simvastatin. The objective of this study was to prepare albumin nanoparticles incorporating simvastatin by the self-assembly method and evaluate their impact on breast cancer metastasis and apoptosis. The data showed the prepared nanoparticles have a diameter of 185 ± 24nm and a drug loading capacity of 8.85 %. The findings exhibit improved release in a lysosomal-like environment and under acidic pH conditions. MTT data showed that nanoparticles do not exhibit a dose-dependent effect on cells. Additionally, the results from MTT, flow cytometry, and qPCR analyses demonstrated that nanoparticles have a greater inhibitory and lethal effect on MDA-MB-231 cells compared to normal simvastatin. And cause cells to accumulate in the G0/G1 phase, initiating apoptotic pathways by inhibiting cell cycle progression. Nanoparticles containing simvastatin can prevent cell invasion and migration in both monolayer and spheroid models, as compared to simvastatin alone, at microscopic levels and in gene expression. The obtained data clearly showed that, compared to simvastatin, nanoparticles containing simvastatin demonstrated significant efficacy in suppressing the growth, proliferation, invasion, and migration of cancer cells in monolayer (2D) and spheroid (3D) models.
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In order to promote the high-value utilization of waste phosphogypsum (PG), hydroxyapatite was directly synthesized from PG by acid precipitation-hydrothermal method (PGHAP), which was used for the adsorption of bovine serum albumin (BSA) and lysozyme (LYS). The synthesized PGHAP was characterized by XRD, SEM, FTIR and BET, and the effects of various factors on protein adsorption capacity were studied. The results showed that PGHAP exhibits a clear needle-like morphology, high crystallinity, and an average size of about 200 nm. The pH had the greatest effect on the adsorption of protein, and the highest adsorption capacity was obtained at pH 4.0. In addition, the adsorption mechanism of protein on PGHAP was explored by adsorption kinetics and adsorption isotherm. The adsorption of protein on PGHAP conforms to the Intra-particle diffusion model kinetic model, the maximum adsorption capacity of protein on PGHAP can reach 31 mg/g, which is comparable to other adsorbents in this field. In addition, the adsorption behaviour of PGHAP on protein is more appropriately described by Langmuir isotherm model, which indicates that the binding site with uniform energy on the surface of PGHAP realizes the monolayer adsorption of protein. The main adsorption mechanisms are ion exchange, co-precipitation, complexation reaction and so on. Therefore, the needle-like PGHAP synthesized from waste PG is a protein adsorbent with industrial application potential.
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Introduction MXenes (Ti3C2) represent a group of two-dimensional inorganic compounds, produced through a top-down exfoliation method. They comprise ultra-thin layers of transition metal carbides, or carbonitrides, and exhibit hydrophilic properties on their surfaces. Utilizing Ti3C2 BiOCl nanoparticles for their antimicrobial and antioxidant attributes involves enhancing synthesis, processing, and characterization techniques. Materials and method To prepare Ti3C2 MXene, dissolve 1.6 g of LiF in 20 ml of 9M HCl. Slowly add 1 g of Ti3AlC2 (titanium aluminum carbide) powder to the solution while stirring. Etch at 35°C for 24 h to remove Al layers from Ti3AlC2, leaving Ti3C2 layers. Wash the mixture with distilled water and ethanol until the pH is around 6. Collect the washed sediment by centrifugation and sonicate it in distilled water for 1 h. Centrifuge to remove unexfoliated particles. For BiOCl synthesis, dissolve 2 mmol of Bi(NO3)3·5H2O (bismuth nitrate pentahydrate) in 10 ml of 2M HCl (hydrochloric acid) with 0.5 g of PVP (polyvinylpyrrolidone). Transfer the solution to a Teflon-lined autoclave, fill it with distilled water up to 80%, and heat at 160°C for 24 h. Collect the precipitate by centrifugation, wash, and dry at 60°C for 12 h. Disperse BiOCl nanoparticles in distilled water, sonicate for 30 min, add Ti3C2 MXene dispersion, stir for 2 h, collect, wash, dry, and calcine at 400°C for 2 h. Result The Scanning Electron Microscope (SEM) utilizes electrons, rather than light, to generate highly magnified images. Energy Dispersive X-ray Spectroscopy (EDS) complements SEM by analyzing the X-ray spectrum emitted when a solid sample is bombarded with electrons, enabling localized chemical analysis. In SEM imaging, incorporating an X-ray spectrometer allows for both element mapping and point analysis. The SEM image of the prepared samples reveals accordion-like multilayer structures in BiOCl, characterized by thin sheet-like structures with numerous pores. EDS, relying on X-ray emissions from electron bombardment, facilitates detailed chemical analysis at specific locations within the sample. Conclusion Our research has shed light on the synthesis and characterization processes of two-dimensional Ti3C2 BiOCl nanoparticles, revealing their remarkable antimicrobial and antioxidant properties.
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This study employs an optimized and environmentally friendly method to extract and purify chondroitin sulfate (CS) from bovine nasal cartilage using enzymatic hydrolysis, ethanol precipitation, and DEAE Sepharose Fast Flow column chromatography. The extracted CS, representing 44.67 % ± 0.0016 of the cartilage, has a molecular weight of 7.62 kDa. Characterization through UV, FT-IR, NMR spectroscopy, and 2-aminoacridone derivatization HPLC revealed a high content of sulfated disaccharides, particularly ΔDi4S (73.59 %) and ΔDi6S (20.61 %). Interaction studies with bovine serum albumin (BSA) using fluorescence spectroscopy and molecular docking confirmed a high-affinity, static quenching interaction with a single binding site, primarily mediated by van der Waals forces and hydrogen bonding. The interaction did not significantly alter the polarity or hydrophobicity of BSA aromatic amino acids. These findings provide a strong foundation for exploring the application of CS in tissue engineering and drug delivery systems, leveraging its unique interaction with BSA for targeted delivery and enhanced efficacy.
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Sulfatos de Condroitina , Cartílagos Nasales , Albúmina Sérica Bovina , Animales , Bovinos , Sulfatos de Condroitina/química , Simulación del Acoplamiento Molecular , Peso Molecular , Cartílagos Nasales/química , Cartílagos Nasales/metabolismo , Unión Proteica , Albúmina Sérica Bovina/químicaRESUMEN
The translation of silver-based nanotechnology 'from bench to bedside' requires a deep understanding of the molecular aspects of its biological action, which remains controversial at low concentrations and non-spherical morphologies. Here, we present a hemocompatibility approach based on the effect of the distinctive electronic charge distribution in silver nanoparticles (nanosilver) on blood components. According to spectroscopic, volumetric, microscopic, dynamic light scattering measurements, pro-coagulant activity tests, and cellular inspection, we determine that at extremely low nanosilver concentrations (0.125-2.5µg ml-1), there is a relevant interaction effect on the serum albumin and red blood cells (RBCs). This explanation has its origin in the surface charge distribution of nanosilver particles and their electron-mediated energy transfer mechanism. Prism-shaped nanoparticles, with anisotropic charge distributions, act at the surface level, generating a compaction of the native protein molecule. In contrast, the spherical nanosilver particle, by exhibiting isotropic surface charge, generates a polar environment comparable to the solvent. Both morphologies induce aggregation at NPs/bovine serum albumin ≈ 0.044 molar ratio values without altering the coagulation cascade tests; however, the spherical-shaped nanosilver exerts a negative impact on RBCs. Overall, our results suggest that the electron distributions of nanosilver particles, even at extremely low concentrations, are a critical factor influencing the molecular structure of blood proteins' and RBCs' membranes. Isotropic forms of nanosilver should be considered with caution, as they are not always the least harmful.
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Eritrocitos , Nanopartículas del Metal , Albúmina Sérica Bovina , Plata , Plata/química , Nanopartículas del Metal/química , Eritrocitos/metabolismo , Eritrocitos/química , Humanos , Albúmina Sérica Bovina/química , Albúmina Sérica Bovina/metabolismo , Propiedades de Superficie , Animales , Bovinos , Coagulación Sanguínea/efectos de los fármacos , Proteínas Sanguíneas/metabolismo , Proteínas Sanguíneas/química , Ensayo de MaterialesRESUMEN
Glioblastoma (GBM) is the most common and aggressive malignant brain tumor. Standard therapy includes maximal surgical resection, radiotherapy, and adjuvant temozolomide (TMZ) administration. However, the rapid development of TMZ resistance and the impermeability of the blood-brain barrier (BBB) significantly hinder the therapeutic efficacy. Herein, we developed spatiotemporally controlled microneedle patches (BMNs) loaded with TMZ and niclosamide (NIC) to overcome GBM resistance. We found that hyaluronic acid (HA) increased the viscosity of bovine serum albumin (BSA) and evidenced that concentrations of BSA/HA exert an impact degradation rates exposure to high-temperature treatment, showing that the higher BSA/HA concentrations result in slower drug release. To optimize drug release rates and ensure synergistic antitumor effects, a 15% BSA/HA solution constituting the bottoms of BMNs was chosen to load TMZ, showing sustained drug release for over 28 days, guaranteeing long-term DNA damage in TMZ-resistant cells (U251-TR). Needle tips made from 10% BSA/HA solution loaded with NIC released the drug within 14 days, enhancing TMZ's efficacy by inhibiting the activity of O6-methylguanine-DNA methyltransferase (MGMT). BMNs exhibit superior mechanical properties, bypass the BBB, and gradually release the drug into the tumor periphery, thus significantly inhibiting tumor proliferation and expanding median survival in mice. The on-demand delivery of BMNs patches shows a strong translational potential for clinical applications, particularly in synergistic GBM treatment.
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Glioblastoma , Ácido Hialurónico , Niclosamida , Albúmina Sérica Bovina , Temozolomida , Temozolomida/química , Temozolomida/farmacología , Temozolomida/farmacocinética , Glioblastoma/tratamiento farmacológico , Glioblastoma/patología , Glioblastoma/metabolismo , Animales , Humanos , Ratones , Niclosamida/farmacología , Niclosamida/química , Niclosamida/farmacocinética , Albúmina Sérica Bovina/química , Ácido Hialurónico/química , Línea Celular Tumoral , Resistencia a Antineoplásicos/efectos de los fármacos , Neoplasias Encefálicas/tratamiento farmacológico , Neoplasias Encefálicas/patología , Neoplasias Encefálicas/metabolismo , Agujas , Sistemas de Liberación de Medicamentos/instrumentación , Ratones Desnudos , Liberación de FármacosRESUMEN
Taylor dispersion analysis (TDA) is a rapid and precise method for determining the hydrodynamic radius (RH) of various substances. We present a versatile TDA system with a flow-through sample injection device, two compact 3-in-1 detectors, and a high-voltage power supply. The 3D-printed detectors combine fluorimetry (FD), photometry (AD@255 nm), and contactless conductometry (C4D) in a single head, enabling simultaneous detection at one capillary window. Using bovine serum albumin (BSA) as a model analyte, we compare TDA with different detection methods. BSA labeled with fluorescein isothiocyanate (FITC) is analyzed in both pulse mode and capillary electrophoresis (CE) TDA. FD and AD detection yield similar RH values, except when FITC binds with small ions in the buffer. In phosphate buffer, C4D underestimates RH values by approximately 18 % due to BSA self-association. In Tris-based buffers, C4D values are 87%-96 % of AD values in pulse mode. With CE-TDA using Tris-CHES buffer, no statistical difference is found across all detections. The system is also applied to CE-TDA of various compounds, particularly charged saccharides. CE-TDA improves the accuracy of TDA results from C4D. We demonstrate the resolution of mixed C4D-TDA signals with assistance from FD and AD signals, successfully resolving gluconate peaks fully covered by another compound. The versatile system with 3-in-1 detection offers a powerful tool for TDA of mixtures and enhances sample throughput.
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Fluoresceína-5-Isotiocianato , Fluorometría , Fotometría , Albúmina Sérica Bovina , Albúmina Sérica Bovina/química , Albúmina Sérica Bovina/análisis , Fluorometría/métodos , Bovinos , Fotometría/métodos , Fluoresceína-5-Isotiocianato/química , Animales , Hidrodinámica , Electroforesis Capilar/métodosRESUMEN
The interaction of human proteins and metal species, both ions and nanoparticles, is poorly understood despite their growing importance. These materials are the by-products of corrosion processes and are of relevance for food and drug manufacturing, nanomedicine, and biomedical implant corrosion. Here, we study the interaction of Cr(III) ions and chromium oxide nanoparticles with bovine serum albumin in physiological conditions. This study combined electrophoretic mobility measurements, spectroscopy, and time-of-flight secondary ion mass spectrometry with principal component analysis. It was determined that neither metal species resulted in global albumin unfolding. The Cr(III) ions interacted strongly with amino acids found in previously discovered metal binding sites, but also were most strongly implicated in the interaction with negatively charged acid residues, suggesting an electrostatic interaction. Bovine serum albumin (BSA) was found to bind to the Cr2O3 nanoparticles in a preferential orientation, due to electrostatic interactions between the positive amino acid residues and the negative chromium oxide nanoparticle surface. These findings ameliorate our understanding of the interaction between trivalent chromium ions and nanoparticles, and biological macromolecules.
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Cromo , Nanopartículas , Albúmina Sérica Bovina , Albúmina Sérica Bovina/química , Albúmina Sérica Bovina/metabolismo , Cromo/química , Nanopartículas/química , Bovinos , Animales , Unión Proteica , Iones/química , Electricidad Estática , Sitios de Unión , Humanos , Compuestos de Cromo/químicaRESUMEN
This study explored how high hydrostatic pressure (HHP) and proteins (i.e., BSA and HSA) influence the color and chemical stability of cyanidin-3-O-glucoside (C3G) at neutral pH. HHP treatments (100-500 MPa, 0-20 min, 25 °C) did not affect C3G content in phosphate buffer (PB) and MOPS buffer. However, significant color loss of C3G occurred in PB due to pressure-induced pH reduction (e.g., from 7 to 4.8 at 500 MPa), which accelerated the hydration of C3G, converting it from colored to colorless species. Consequently, MOPS buffer was employed for subsequent stability experiments to assess the impact of protein and HHP on the thermal, storage, and UV light stability of C3G. Initially, rapid color loss occurred during heating and storage, primarily due to the reversible hydration of C3G until equilibrium with colorless species was reached, followed by slower parallel degradation. HSA increased the fraction of colored species at equilibrium but accelerated thermal degradation, while BSA had minimal effects. UV light irradiation accelerated the degradation of C3G colored species, causing direct degradation without conversion to colorless species, a process further intensified by the presence of proteins. HHP exhibited a negligible effect on C3G stability regardless of protein addition. These findings provide insights into anthocyanin stability under HHP and protein interactions, contributing to the development of future formulation and processing strategies for improved stability and broader applications.
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Antocianinas , Color , Glucósidos , Presión Hidrostática , Antocianinas/química , Glucósidos/química , Concentración de Iones de Hidrógeno , Rayos Ultravioleta , Albúmina Sérica Bovina/químicaRESUMEN
Sonosensitizers play a crucial role in the efficacy of sonodynamic antitumor therapy (SDT) and sonodynamic antimicrobial chemotherapy (SACT), highlighting the necessity for the development of new compounds with good sonodynamic activity. In this study, three novel 3-substituted ciprofloxacin derivatives (CIPD1, CIPD2, and CIPD3) were designed and synthesized. Their sonodynamic activities were evaluated by assessing the damage to bovine serum albumin (BSA) and Escherichia coli (E. coli). Furthermore, the potential mechanism underlying their sonodynamic damage activities was investigated by detecting reactive oxygen species (ROS) under ultrasound irradiation (US). The results demonstrated that all three derivatives exhibited enhanced sonodynamic damage to BSA and E. coli under US, with CIPD1 and CIPD2 showing superior effectiveness compared to CIP. Both the concentrations of derivatives and the duration of ultrasound irradiation were found to significantly impact their sonodynamic effects. All three CIP derivates could be activated to produce ROS following ultrasound irradiation, primarily consisting of 1O2 and ·OH. The levels of ROS production were positively correlated with their sonodynamic activities, potentially explaining the mechanism underlying their sonodynamic damage activities.
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Ciprofloxacina , Escherichia coli , Especies Reactivas de Oxígeno , Albúmina Sérica Bovina , Ciprofloxacina/farmacología , Ciprofloxacina/química , Especies Reactivas de Oxígeno/metabolismo , Escherichia coli/efectos de los fármacos , Albúmina Sérica Bovina/química , Ondas Ultrasónicas , Animales , Antibacterianos/farmacología , Antibacterianos/química , Antibacterianos/síntesis químicaRESUMEN
Molecular interaction of entecavir (ETV) with the transport protein, albumin from bovine serum (BSA) was explored through multispectral and molecular docking approaches. The BSA fluorescence was appreciably quenched upon ETV binding and the quenching nature was static. The ETV-BSA complexation and the static quenching process were further reiterated using UV-visible absorption spectra. The binding constant (Ka) values of the complex were found as 1.47 × 104-4.0 × 103 M-1, which depicting a modarate binding strength in the ETV-BSA complexation. The experimental outcomes verified that the stable complexation was primarily influenced by hydrophobic interactions, hydrogen bonds and van der Waals forces. Synchronous and 3-D fluorescence spectral results demonstrated that ETV had significant impact on the hydrophobicity and polarity of the molecular environment near Tyr and Trp residues. Competitive site-markers displacement (with warfarin and ketoprofen) results discovered the suitable binding locus of ETV at site I in BSA. The molecular docking assessments also revealed that ETV formed hydrogen bonds and hydrophobic interactions with BSA, predominantly binding to site I (sub-domain IIA) of BSA.
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Antivirales , Guanina , Simulación del Acoplamiento Molecular , Albúmina Sérica Bovina , Espectrometría de Fluorescencia , Albúmina Sérica Bovina/química , Albúmina Sérica Bovina/metabolismo , Guanina/química , Guanina/análogos & derivados , Antivirales/química , Antivirales/farmacología , Animales , Bovinos , Unión Proteica , Sitios de Unión , Interacciones Hidrofóbicas e Hidrofílicas , Espectrofotometría Ultravioleta , Enlace de HidrógenoRESUMEN
Influenza remains a global public health threat, and the development of new antivirals is crucial to combat emerging drug-resistant influenza strains. In this study, we report the synthesis and evaluation of a sialyl lactosyl (TS)-bovine serum albumin (BSA) conjugate as a potential multivalent inhibitor of the influenza virus. The key trisaccharide component, TS, was efficiently prepared via a chemoenzymatic approach, followed by conjugation to dibenzocyclooctyne-modified BSA via a strain-promoted azide-alkyne cycloaddition reaction. Biophysical and biochemical assays, including surface plasmon resonance, isothermal titration calorimetry, hemagglutination inhibition, and neuraminidase inhibition, demonstrated the strong binding affinity of TS-BSA to the hemagglutinin (HA) and neuraminidase (NA) proteins of the influenza virus as well as intact virion particles. Notably, TS-BSA exhibited potent inhibitory activity against viral entry and release, preventing cytopathic effects in cell culture. This multivalent presentation strategy highlights the potential of glycocluster-based antivirals for combating influenza and other drug-resistant viral strains.