This article presents results on the aggregation and disaggregation kinetics on a 1 μm diameter charged superparamagnetic particles dispersed in water under a constant uniaxial magnetic field in experiments with salt (KCl) added to the suspension in order to observe the behaviour of the system when the electrical properties of the particles have been screened. These particles have an electric charge and are confined between two separated 100 μm thick quartz windows, and sediment near the charged bottom wall. The electrostatic interactions that take place in this experimental setup may affect the micro-structure and colloidal stability of the suspension and thus, the dynamics of aggregation and disaggregation.
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http://dx.doi.org/10.1140/epje/i2011-11036-5 | DOI Listing |
Alzheimers Dement
December 2024
Tel Aviv university, Tel Aviv, Israel, Israel.
Background: Amyloid filaments formation is a complex kinetic and thermodynamic process. The dependence of peptide polymerization on peptide-peptide interactions to form a β-pleated sheet fibrils and the stimulatory influence of other proteins on the reaction suggest that amyloid formation may be subject to modulation METHOD: In vitro formation of β-amyloid was induced by incubation of an aqueous solution of AβP (10 mg/ml) for 7 days at 37°C. The extent of β-amyloid formation and disaggregation were monitored using a panel of well characterized mAbs raised against soluble AβP fragments.
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December 2024
Department of Biophysics, Faculty of Environmental Biology, University of Life Sciences in Lublin, Akademicka 13, 20-950, Lublin, Poland.
We present a comprehensive spectroscopic study supported by theoretical quantum chemical calculations conducted on a molecular system (4-(5-methyl-1,3,4-thiadiazol-2-yl)benzene-1,3-diol (C1) and the antibiotic Amphotericin B (AmB)) that exhibits highly synergistic properties. We previously reported the strong synergism of this molecular system and now wish to present related stationary measurements of UV-Vis absorption, fluorescence, and fluorescence anisotropy in a polar, aprotic solvent (DMSO and a PBS buffer), followed by time-resolved fluorescence intensity and anisotropy decay studies using different ratios of the selected 1,3,4-thiadiazole derivative to Amphotericin B. Absorption spectra measured for the system revealed discrepancies in terms of the shapes of absorption bands, particularly in PBS.
View Article and Find Full Text PDFBackground: Cardiovascular disease (CVD) prevalence varies widely among Asian American adults. The American Heart Association added healthy sleep to its metrics to define ideal cardiovascular health. Little is known about the association between sleep and CVD prevalence among Asian subgroups.
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December 2024
Division of Applied Mathematics, Brown University, Providence, Rhode Island, United States.
Gaucher Disease (GD) is a rare genetic disorder characterized by a deficiency in the enzyme glucocerebrosidase, leading to the accumulation of glucosylceramide in various cells, including red blood cells (RBCs). This accumulation results in altered biomechanical properties and rheological behavior of RBCs, which may play an important role in blood rheology and the development of bone infarcts, avascular necrosis (AVN) and other bone diseases associated with GD. In this study, dissipative particle dynamics (DPD) simulations are employed to investigate the biomechanics and rheology of blood and RBCs in GD under various flow conditions.
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November 2024
Medical Bionanotechnology, Faculty of Allied Health Sciences, Chettinad Hospital and Research Institute, Chettinad Academy of Research and Education, Chettinad Health City, Kelambakkam, Chennai-603103, India.
Background And Purpose: Amyloidosis is a group of diseases including diabetes type II and neurological disorders, such as Alzheimer's disease, Parkinson's disease, prion disease, etc., where a common trait is observed; accumulation of misfolded protein at different parts of the body, especially the brain which manifests the typical symptoms like dementia, movement disorders, etc. These misfolded proteins, named amyloids, are protease resistant and thus it becomes difficult to manage these diseases in vivo.
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