Search results for: BSA | bovine serum albumin
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Human knockout cerebral organoids: A model system for testing AAV9-mediated gene therapy for reducing GM1 ganglioside storage in GM1 gangliosidosis.GM1 gangliosidosis is an autosomal recessive neurodegenerative disorder caused by the deficiency of lysosomal β-galactosidase (β-gal) and resulting in accumulation of GM1 ganglioside. The disease spectrum ranges from infantile to late onset and is uniformly fatal, with no effective therapy currently available. Although animal models have been useful for understanding disease pathogenesis and exploring therapeutic targets, no relevant human central nervous system (CNS) model system has been available to study its early pathogenic events or test therapies. To develop a model of human GM1 gangliosidosis in the CNS, we employed CRISPR/Cas9 genome editing to target exons 2 and 6, common sites for mutations in patients, to create isogenic induced pluripotent stem (iPS) cell lines with lysosomal β-gal deficiency. We screened for clones with <5% of parental cell line β-gal enzyme activity and confirmed knockout clones using DNA sequencing. We then generated knockout cerebral organoids from one of these knockout iPS cell clones. Analysis of knockout organoids in culture revealed progressive accumulation of GM1 ganglioside. knockout organoids microinjected with AAV9-GLB1 vector showed a significant increase in β-gal activity and a significant reduction in GM1 ganglioside content compared with AAV9-GFP-injected organoids, demonstrating the efficacy of an AAV9 gene therapy-based approach in GM1 gangliosidosis. This proof-of-concept in a human cerebral organoid model completes the pre-clinical studies to advance to clinical trials using the AAV9-GLB1 vector.
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Magnetically controlled protein nanocontainers as a drug depot for the hemostatic agent.Currently, there is a number of successfully implemented local hemostatic agents for external bleedings in forms of wound dressings and other topical materials. However, little has been done in the field of intravenous hemostatic agents. Here, we propose a new procedure to fabricate biocompatible protein nanocontainers (NCs) for intravenous injection allowing magneto-controllable delivery and short-term release of the hemostatic agent ε-aminocaproic acid (EACA).
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Design and Construction of Aroyl-Hydrazone Derivatives: Synthesis, Crystal Structure, Molecular Docking and Their Biological Activities.Here, we report synthesis and characterization of four new aroyl-hydrazone derivatives; L 1 -L 4 and their structural as well as biological activities have been explored. In addition to docking with Bovine serum albumin (BSA) and duplex DNA, the experimental results demonstrate the effective binding of L 1 -L 4 with BSA protein and calf thymus DNA (ct-DNA) which is in agreement with the docking results. Further biological activities of L 1 -L 4 have been examined through molecular docking with different proteins which are involved in the propagation of viral or cancer diseases. L 1 shows best binding affinity with Influenza A virus polymerase PB2 subunit (2VY7) with binding energy -11.42 Kcal/mol and inhibition constant 4.23nM whereas L 2 strongly bind with the hepatitis C virus NS5B polymerase (2WCX) with binding energy -10.47 Kcal/mol and inhibition constant 21.06nM. Ligand L 3 binds strongly with TGF-beta receptor 1(3FAA) and L 4 with cancer-related EphA2 protein kinases (1MQB) with binding energy -10.61 Kcal/mol, -10.02 Kcal/mol and inhibition constant 16.67nM and 45.41nM respectively. The binding energies of L 1 -L 4 are comparable with binding energies of their proven inhibitors. L 1 , L 3 and L 4 can be consider as both 3FAA and 1MQB dual targeting anticancer agents, while L 1 and L 3 are both 2VY7 and 2WCX dual targeting antiviral agents. On the other side, L 2 and L 4 target only one virus related target (2WCX). Furthermore, the geometry optimizations of L 1 -L 4 were performed via density functional theory (DFT). Moreover, all four ligands ( L 1 -L 4 ) were characterized by NMR, FTIR, ESI-MS, elemental analysis and their molecular structures were validated by single crystal X-ray diffraction studies.
1155 related Products with: Design and Construction of Aroyl-Hydrazone Derivatives: Synthesis, Crystal Structure, Molecular Docking and Their Biological Activities.Androgen Receptor (Ab 650 Androgen Receptor , Mouse (5α,16β)-N-Acetyl-16-ac Androst-4-ene-3,17-dion-1 Androstadienone C19H26O C Androstane-3a, 17b-diol 5 Androgen Receptor (Ab 650 ∆1-Androstene-3β,17β- Androgen Receptor (Phosph Androgen Receptor Ab-1 An Andrographolide C20H30O5 rac Androst-16-en-2,2,5,6
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C/EBPα deficiency in podocytes aggravates podocyte senescence and kidney injury in aging mice.Kidney aging leads to an increased incidence of end-stage renal disease (ESRD) in the elderly, and aging is a complex biological process controlled by signaling pathways and transcription factors. Podocyte senescence plays a central role in injury resulting from kidney aging. Here, we demonstrated the critical role of C/EBPα in podocyte senescence and kidney aging by generating a genetically modified mouse model of chronological aging in which C/EBPα was selectively deleted in podocytes and by overexpressing C/EBPα in cultured podocytes, in which premature senescence was induced by treatment with adriamycin. Moreover, we illuminated the mechanisms by which podocyte senescence causes tubular impairment by stimulating HK-2 cells with bovine serum albumin (BSA) and chloroquine. Our findings suggest that C/EBPα knockout in podocytes aggravates podocyte senescence through the AMPK/mTOR pathway, leading to glomerulosclerosis, and that subsequent albuminuria exacerbates the epithelial-mesenchymal transdifferentiation of senescent tubular cells by suppressing autophagy. These observations highlight the importance of C/EBPα as a new potential target in kidney aging.
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Effect of Process Parameters on the Initial Burst Release of Protein-Loaded Alginate Nanospheres.The controlled release or delivery of proteins encapsulated in micro/nanospheres is an emerging strategy in regenerative medicine. For this, micro/nanospheres made from alginate have drawn considerable attention for the use as a protein delivery device because of their mild fabrication process, inert nature, non-toxicity and biocompatibility. Though promising, one key issue associated with using alginate micro/nanospheres is the burst release of encapsulated protein at the beginning of the release, which may be responsible for exerting toxic side effects and poor efficiency of the delivery device. To address this issue, this study aimed to investigate the effect of process parameters of fabricating protein-loaded alginate nanospheres on the initial burst release. The alginate nanospheres were prepared via a combination of water-in-oil emulsification and the external gelation method and loaded with bovine serum albumin (BSA) as a model protein. The examined process parameters included alginate concentration, ionic cross-linking time and drying time. Once fabricated, the nanospheres were then subjected to the examination of BSA release, as well as the characterization of their morphology, size, and encapsulation efficiency. Our results revealed that by properly adjusting the process parameters, the initial burst release can be reduced by 13%. Taken together, our study demonstrates that regulating process parameters of fabricating alginate nanospheres is a possible means to reduce the initial burst release.
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Albumin-bioinspired iridium oxide nanoplatform with high photothermal conversion efficiency for synergistic chemo-photothermal of osteosarcoma.Protein-based nanocarriers with inherent biocompatibility have been widely served as building blocks to construct versatile therapeutic nanoplatforms. Herein, bovine serum albumin-iridium oxide nanoparticles (denoted BSA-IrO NPs) are successfully synthesized one-step biomineralization approach. The BSA-IrO NPs exhibits uniform size (40 nm), superb biocompatibility and high drug loading capacity for doxorubicin (27.4 wt%). Under near-infrared (NIR) laser irradiation, the as-prepared BSA-IrO NPs exhibited high photothermal conversion ability (54.3%) and good photostability. The drug release experiments displayed pH and NIR laser -triggered DOX release profiles, which could enhance the therapeutic anticancer effect. By utilizing this DOX loaded nanoplatform, effective synergistic chemo-photothermal therapy against human osteosarcoma can be realized, which has been systematically verified both and . Notably, pharmacokinetics studies showed that BSA-IrO@DOX had prolonged blood circulation time due to the BSA component can improve the stealthiness of the nanoparticles during the blood circulation. Meanwhile, and toxicity studies demonstrated that the BSA-IrO NPs can act as biocompatible agents for drug delivery and cancer therapy. Therefore, this work presents a biomineralized iridium-based NPs with remarkable features and be used as a very potential therapeutic nanoplatform for cancer treatment.
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O2-Generating Meta-Organic Frameworks-Based Hydrophobic Photosensitizer Delivery System for Enhanced Photodynamic Therapy.Photodynamic therapy (PDT) has introduced as photochemical processes for treatment by causing cancer cell death and necrosis, with higher accuracy and few side effects. However, the hydrophobicity of most photosensitizers and hypoxia at the tumor sites are two crucial problems to be solved in leading to a successful PDT. Herein, we designed and constructed a novel metal-organic framework-based drug delivery system (BSA-MnO2/Ce6@ZIF-8) with tumor microenvironment (TME)-controllability. In our system, the hydrophobic photosensitizer chlorin e6 (Ce6) was one-pot incorporated into the matrix of zeolitic imidazolate framework 8 (ZIF-8) to form Ce6@ZIF-8 compound, which can efficiently keep the Ce6 molecules isolated and avoid them self-aggregation, and the loading rate of Ce6 was high up to 28.3 wt.%. The bovine serum albumin (BSA)-MnO2 nanoparticles (NPs) with catalase-like activity were loaded onto the surface of ZIF-8, thus had the capacity for self-sufficiency of O2 under the circumstance of H2O2 in acid solution, relieving hypoxia in cancer cells and thereby improving PDT efficiency greatly when irradiated by low power density (230 mW/cm2) 650 nm light. Moreover, the MnO2 NPs can react with H2O2 in acid solution to produce Mn2+, granting the system the qualification of contrast agent for magnetic resonance imaging (MRI). Therefore, our nanoplatform would further contribute to the treatment of hypoxic tumor in clinical practice.
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Raising antibodies against epoxyscillirosidine, the toxic principle contained in Moraea pallida Bak. (Iridaceae), in rabbits.Moraea pallida Bak. (yellow tulp) poisoning is the most important plant cardiac glycoside toxicosis in South Africa. The toxic principle, a bufadienolide, is 1α, 2α-epoxyscillirosidine. The aim was to investigate the potential to develop a vaccine against epoxyscillirosidine. Epoxyscillirosidine, proscillaridin and bufalin, were successfully conjugated to hen ovalbumin (OVA), bovine serum albumin (BSA) and keyhole limpet haemocyanin (KLH). There was a low immune response following vaccination of adult male New Zealand White rabbits with epoxyscillirosidine-OVA (n = 3) and OVA (n = 3) using Freund's adjuvant in Trial (T) 1. The immune response improved significantly in T2 following doubling of the dose to 0.8 mg/rabbit and changing the adjuvant to Montanide. In T3, the rabbits (n = 15), allocated into 5 equal groups, vaccinated with proscillaridin-BSA, bufalin-BSA, epoxyscillirosidine-KLH, epoxyscillirosidine-BSA and BSA respectively, using Montanide adjuvant, developed antibodies against the administered immunogens, with epoxyscillirosidine-KLH inducing the highest immune response. Proscillaridin and bufalin antibodies cross-reacted with epoxyscillirosidine in an enzyme linked immunosorbent assay. The conjugation methodology will be adjusted in the future to target optimal conjugation efficiency. Additional vaccination will be conducted in search of neutralizing antibodies against the yellow tulp toxin. The cross-reactivity of proscillaridin and bufalin antibodies with epoxyscillirosidine could be studied in future to explore the potential to prevent yellow tulp poisoning.
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Comparative refolding of guanidinium hydrochloride denatured bovine serum albumin assisted by cationic and anionic surfactants via artificial chaperone protocol: Biophysical insight.In the present study, we report the cooperative refolding/renaturation behaviour of guanidinium hydrochloride (GdnHCl) denatured bovine serum albumin (BSA) in the presence of cationic surfactant cetyltrimethylammonium bromide (CTAB), anionic surfactant sodium dodecyl sulphate (SDS) and their catanionic mixture in the solution of 60 mM sodium phosphate buffer of physiological pH 7.4, using artificial chaperone-assisted two-step method. Here, we have employed biophysical techniques to characterize the refolding mechanism of denatured BSA after 200 times of dilution in the presence of cationic, anionic surfactants and their catanionic mixture, separately. We have found that minimum refolding of diluted BSA in the presence of 1:1 rational mixture of CTAB and SDS (CTAB/SDS = 50/50), it may be due to the micelles formation which is responsible for the unordered microstructure aggregate formation. Other mixtures (CTAB/SDS = 20/80 and 80/20) slightly played an effective role during refolding process in the presence of methyl-β-cyclodextrin. On other hand, CTAB and SDS are more effective and reflect a good renaturation tendency of denatured BSA solution separately and in existence of methyl-β-cyclodextrin as compare to their mixture compositions. But overall, CTAB has the better renaturation tendency as compare to SDS in the existence of methyl-β-cyclodextrin. These results ascribed the presence of charge head group and length of hydrophobic tail of CTAB surfactant that plays an important task during electrostatic and hydrophobic interactions at pH 7.4 at which BSA carries negative charge on their surface. These biophysical parameters suggest that, CTAB surfactant assisted artificial chaperone protocol may be utilized in the protein renaturation/refolding studies, which may address the associated problems of biotechnological industries for the development of efficient and inexpensive folding aides, which may also be used to produced genetically engineered cells related diseases, resulting from protein misfolding/aggregation.
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Influence of protein conformation and selected Hofmeister salts on bovine serum albumin/lutein complex formation.Protein conformation and the 3D water structure play important roles in the ability of bovine serum albumin (BSA) to form stable nanostructures with bioactive molecules. We studied the influence of BSA unfolding and those of two Hofmeister salts, sodium chloride (NaCl) as kosmotrope and sodium thiocyanate (NaSCN) as chaotrope, on BSA/lutein binding at pH 7.4 using fluorescence spectroscopy. The BSA/lutein complex formation was entropically driven and lutein was preferentially bound to site III of BSA. The binding constant (10 L mol), complex stoichiometry (1:1), and thermodynamic potential for BSA/lutein binding were independent of protein conformation and Hofmeister salts. However, the enthalpic and entropic components of BSA/lutein binding in the presence of NaSCN decreased as the temperature increased. The opposite was observed for BSA/lutein binding in the presence of NaCl and for denatured BSA/lutein binding. Therefore, the BSA conformation and 3D water structure directly affected the BSA/lutein binding thermodynamics.
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