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Journal of Ayurveda and Integrative... 2023Rheumatoid arthritis (RA) is an inflammation of joints with increased cellularity of synovial tissue. Allopathic drugs possess several adverse effects, which have led to...
BACKGROUND
Rheumatoid arthritis (RA) is an inflammation of joints with increased cellularity of synovial tissue. Allopathic drugs possess several adverse effects, which have led to increase in the utilization of herbal medicines. Polyherbal emulgel resolves the bioavailability issue associated with hydrophobic drugs and can be used effectively in the treatment of RA.
OBJECTIVES
The present study aimed at the formulation of polyherbal emulgel, and evaluation of in vitro anti-inflammatory activity and in vivo antiarthritic activity.
METHODS
Seven emulgels F-1 to F-7 were optimally formulated. In vitro anti-inflammatory activity was determined using protein denaturation method employing Diclofenac sodium as the standard. In antiarthritic study Complete Freund's Adjuvant (CFA) model was used. The various parameters were assessed, like paw volume, body weight, hematological parameters, antioxidant parameters, Rheumatic factor (RF), and histopathological study of ankle joint.
RESULTS
F-4 and F-7 were found to be optimized formulations as compared to other formulations. The in vitro anti-inflammatory activity was found to be highest in F-4 with IC 7.74 and F-7 with IC 8.87 in comparison with Diclofenac sodium having IC 57.0. Both formulations F-7 and F-4 showed a significant reduction in paw volume and normalization of body weights. The formulation F-7 even showed more potent antiarthritic activity than F-4 by decreasing white blood cells (WBC), lymphocytes, increasing packed cell volume (PCV), neutrophils, superoxide dismutase (SOD), catalase and decreasing malondialdehyde (MDA) levels in serum. This was further confirmed by histopathological study.
CONCLUSION
As an anti-inflammatory agent, this newly developed emulgel was found to possess more therapeutic efficacy than commercially available diclofenac sodium.
PubMed: 38016365
DOI: 10.1016/j.jaim.2023.100828 -
Critical Reviews in Food Science and... 2024Freezing is commonly used to extend the shelf life of meat and meat products but may impact the overall quality of those products by inducing structural changes in... (Review)
Review
Freezing is commonly used to extend the shelf life of meat and meat products but may impact the overall quality of those products by inducing structural changes in myofibrillar proteins (MPs) through denaturation, chemical modification, and encouraging protein aggregation. This review covers the effect of freezing on the denaturation of MPs in terms of the effects of ice crystallization on solute concentrations, cold denaturation, and protein oxidation. Freezing-induced denaturation of MPs begins with ice crystallization in extracellular spaces and changes in solute concentrations in the unfrozen water fraction. At typical temperatures for freezing meat (lower than -18 °C), cold denaturation of proteins occurs, accompanied by an alteration in their secondary and tertiary structure. Moreover, the disruption of muscle cells triggers the release of cellular enzymes, accelerating protein degradation and oxidation. To minimize severe deterioration during the freezing and frozen storage of meat, there is a vital need to use an appropriate freezing temperature below the glass transition temperature and to avoid temperature fluctuations during storage to prevent recrystallization. Such an understanding of MP denaturation can be applied to determine the optimum freezing conditions for meat products with highly retained sensory, nutritional, and functional qualities.
Topics: Freezing; Ice; Proteins; Meat; Water
PubMed: 36052640
DOI: 10.1080/10408398.2022.2116557 -
Journal of Dairy Science Aug 2023Gastric digestion of 2 commercial ultrafiltered milks and milk enriched with skim milk powder (to simulate concentration by reverse osmosis) was investigated and...
Gastric digestion of 2 commercial ultrafiltered milks and milk enriched with skim milk powder (to simulate concentration by reverse osmosis) was investigated and compared with the digestion of nonconcentrated milk. Curd formation and proteolysis of high-protein milks in simulated gastric conditions were studied using oscillatory rheology, extrusion testing, and gel electrophoresis. The presence of pepsin in the gastric fluid triggered coagulation at pH >6 and the elastic modulus of gels from high-protein milks was ~5 times larger than the gel from reference milk. Despite similar protein concentrations, the coagulum from milk enriched with skim milk powder showed higher resistance to shear deformation than the coagula from ultrafiltered milks. The gel structure was also more heterogeneous. During digestion, the degradation of coagula from high-protein milks was slowed down compared with the coagulum from reference milk, and intact milk proteins were still detected after 120 min. Differences in the digestion patterns of coagula from high-protein milks were observed and were associated with the proportion of minerals bound to caseins and the denaturation rate of whey proteins.
Topics: Animals; Proteolysis; Powders; Milk; Milk Proteins; Whey Proteins; Caseins; Rheology; Hydrogen-Ion Concentration
PubMed: 37291035
DOI: 10.3168/jds.2022-22714 -
Circulation. Heart Failure May 2024
PubMed: 38602111
DOI: 10.1161/CIRCHEARTFAILURE.124.011623 -
ACS Nano Nov 2023The application of fluorescent proteins (FPs) in optoelectronics is hindered by the need for effective protocols to stabilize them under device preparation and...
The application of fluorescent proteins (FPs) in optoelectronics is hindered by the need for effective protocols to stabilize them under device preparation and operational conditions. Factors such as high temperatures, irradiation, and organic solvent exposure contribute to the denaturation of FPs, resulting in a low device performance. Herein, we focus on addressing the photoinduced heat generation associated with FP motion and rapid heat transfer. This leads to device temperatures of approximately 65 °C, causing FP-denaturation and a subsequent loss of device functionality. We present a FP stabilization strategy involving the integration of electrostatically self-assembled FP-apoferritin cocrystals within a silicone-based color down-converting filter. Three key achievements characterize this approach: () an engineering strategy to design positively supercharged FPs (+22) without compromising photoluminescence and thermal stability compared to their native form, () a carefully developed crystallization protocol resulting in highly emissive cocrystals that retain the essential photoluminescence features of the FPs, and () a strong reduction of the device's working temperature to 40 °C, leading to a 40-fold increase in Bio-HLEDs stability compared to reference devices.
PubMed: 37902649
DOI: 10.1021/acsnano.3c05284 -
Current Opinion in Gastroenterology Sep 2023Patients with pancreatic tumors may have limited treatment options. Pancreatic tumor ablation is a novel and emerging treatment modality which can now be performed using... (Review)
Review
PURPOSE OF REVIEW
Patients with pancreatic tumors may have limited treatment options. Pancreatic tumor ablation is a novel and emerging treatment modality which can now be performed using endoscopic ultrasound (EUS) guidance. This modality is well suited to guide energy delivery for radiofrequency ablation (RFA) and microwave ablation. These approaches provide minimally invasive, nonsurgical methods for delivering energy to ablate pancreatic tumors in situ . This review summarizes the current data and safety profile for ablation in managing pancreatic cancer and pancreatic neuroendocrine tumors.
RECENT FINDINGS
RFA uses thermal energy to induce cell death by coagulative necrosis and protein denaturation. Studies have reported increased overall survival in patients with pancreatic tumors treated with EUS-guided RFA in a multimodality systemic approach and when used in palliative surgeries. Radiofrequency ablation may have corollary benefits in inducing an immune-modulatory effect. Tumor marker carbohydrate antigen 19-9 has been reported to decrease in response to RFA. Microwave ablation is an emerging modality.
SUMMARY
RFA utilizes focal thermal energy to induce cell death. RFA has been applied through open, laparoscopic, and radiographic modalities. EUS-guided approaches are now allowing RFA and microwave ablation to be performed for pancreatic tumors in situ .
Topics: Humans; Pancreatic Neoplasms; Radiofrequency Ablation; Pancreas; Endosonography; Laparoscopy; Catheter Ablation
PubMed: 37097824
DOI: 10.1097/MOG.0000000000000939 -
Biomacromolecules Nov 2023Proteins are commonly encapsulated in alginate gels for drug delivery and tissue-engineering applications. However, there is limited knowledge of how encapsulation...
Proteins are commonly encapsulated in alginate gels for drug delivery and tissue-engineering applications. However, there is limited knowledge of how encapsulation impacts intrinsic protein properties such as folding stability or unfolding kinetics. Here, we use fast relaxation imaging (FReI) to image protein unfolding in situ in alginate hydrogels after applying a temperature jump. Based on changes in the Förster resonance energy transfer (FRET) response of FRET-labeled phosphoglycerate kinase (PGK), we report the quantitative impact of multiple alginate hydrogel concentrations on protein stability and folding dynamics. The gels stabilize PGK by increasing its melting temperature up to 18.4 °C, and the stabilization follows a nonmonotonic dependence on the alginate density. In situ kinetic measurements also reveal that PGK deviates more from two-state folding behavior in denser gels and that the gel decreases the unfolding rate and accelerates the folding rate of PGK, compared to buffer. Phi-value analysis suggests that the folding transition state of an encapsulated protein is structurally similar to that of folded protein. This work reveals both beneficial and negative impacts of gel encapsulation on protein folding, as well as potential mechanisms contributing to altered stability.
Topics: Hydrogels; Protein Folding; Protein Stability; Kinetics; Temperature; Protein Denaturation
PubMed: 37906737
DOI: 10.1021/acs.biomac.3c00764 -
The Journal of Physical Chemistry. B Jul 2023Studying protein interactions at low temperatures has important implications for optimizing cryostorage processes of biological tissue, food, and protein-based drugs....
Studying protein interactions at low temperatures has important implications for optimizing cryostorage processes of biological tissue, food, and protein-based drugs. One of the major issues is related to the formation of ice nanocrystals, which can occur even in the presence of cryoprotectants and can lead to protein denaturation. The presence of ice nanocrystals in protein solutions poses several challenges since, contrary to microscopic ice crystals, they can be difficult to resolve and can complicate the interpretation of experimental data. Here, using a combination of small- and wide-angle X-ray scattering (SAXS and WAXS), we investigate the structural evolution of concentrated lysozyme solutions in a cryoprotected glycerol-water mixture from room temperature ( = 300 K) down to cryogenic temperatures ( = 195 K). Upon cooling, we observe a transition near the melting temperature of the solution ( ≈ 245 K), which manifests both in the temperature dependence of the scattering intensity peak position reflecting protein-protein length scales (SAXS) and the interatomic distances within the solvent (WAXS). Upon thermal cycling, a hysteresis is observed in the scattering intensity, which is attributed to the formation of nanocrystallites in the order of 10 nm. The experimental data are well described by the two-Yukawa model, which indicates temperature-dependent changes in the short-range attraction of the protein-protein interaction potential. Our results demonstrate that the nanocrystal growth yields effectively stronger protein-protein attraction and influences the protein pair distribution function beyond the first coordination shell.
Topics: Ice; Scattering, Small Angle; X-Ray Diffraction; Freezing; Solvents; Solutions
PubMed: 37399586
DOI: 10.1021/acs.jpcb.3c02413 -
Foods (Basel, Switzerland) Nov 2023The issue of the short microbiological shelf life of residues from the plant-based beverage industry creates a large food waste problem. Today, the oat beverage residue,...
The issue of the short microbiological shelf life of residues from the plant-based beverage industry creates a large food waste problem. Today, the oat beverage residue, in this study referred to as , is generally converted to energy or used as animal feed. High-pressure pasteurization (200 MPa, 400 MPa, and 600 MPa) was applied to oat okara to investigate the effect on shelf life and microbiological activity. A 4-week microbiological storage study was performed and thermal properties, viscosity, and water and oil holding capacities were analyzed. The total aerobic count, including yeast and mold, was significantly reduced ( < 0.05) by 600 MPa after four weeks of storage at 4 °C. The content of lactic acid bacteria after four weeks of storage was low for untreated oat okara (3.2 log CFU/g) but, for 600 MPa, the content remained at the detection limit (2.3 log CFU/g). Conversely, the treatments of 200 MPa and 400 MPa increased the microbial content of the total aerobic count significantly ( < 0.05) after two weeks in comparison to untreated oat okara. The thermal properties of untreated and high-pressure-treated oat okara demonstrated an increase in protein denaturation of the 12S globulin, avenalin, when higher pressure was applied (400-600 MPa). This was also confirmed in the viscosity measurements where a viscosity peak for avenalin was only present for untreated and 200 MPa treated oat okara. The water holding capacity did not change as a function of high-pressure treatment (3.5-3.8 mL/g) except for the treatment at 200 MPa, which was reduced (2.7 mL/g). The oil holding capacity was constant (1.2-1.3 mL/g) after all treatments. High-pressure pasteurization of 600 MPa reduced the microbial content in oat okara resulting in a shelf life of 2-4 weeks. However, more research is required to identify the microorganisms in oat okara to achieve a microbiologically safe product that can be used for food applications.
PubMed: 38002127
DOI: 10.3390/foods12224070