Synthesis, Tunable Multicolor Output, and High Pure Red Upconversion Emission of Lanthanide-Doped Lu2O3 Nanosheets

Yb3+ and Ln3+ (Ln = Er, Ho) codoped Lu2O3 square nanocubic sheets were successfully synthesized via a facile hydrothermal method followed by a subsequent dehydration process. The crystal phase, morphology, and composition of hydroxide precursors and target oxides were characterized by X-ray diffraction (XRD), field emission scanning electron microscope (FE-SEM), and energy-dispersive X-ray spectroscope (EDS). Results present the as-prepared Lu2O3 crystallized in cubic phase, and the monodispersed square nanosheets were maintained both in hydroxide and oxides. Moreover, under 980 nm laser diode (LD) excitation, multicolor output from red to yellow was realized by codoped different lanthanide ions in Lu2O3. It is noteworthy that high pure strong red upconversion emission with red to green ratio of 443.3 of Er-containing nanocrystals was obtained, which is beneficial for in vivo optical bioimaging

Synthesis of a starch-composite magnetic material modified with polyethyleneimine for enhanced adsorption of diclofenac sodium, methyl orange, Amaranth, and hexavalent chromium

This study introduces Magnetic Starch (MAST), an innovative material designed for the efficient and rapid removal of water contaminants. MAST is synthesized by integrating polyethyleneimine and magnetic Fe3O4 nanoparticles into a starch composite. It exhibits a saturation magnetization of 7.3 emu/g and a functional surface area of 3.55 m² g−1. MAST's amine group density is 12.03 mmol/g, indicating a strong affinity for pollutants. Notably, MAST demonstrates exceptional adsorption capacities for various hazardous substances, including diclofenac sodium (620.51 mg g−1), methyl orange (470.85 mg g−1), amaranth (193.71 mg g−1), and hexavalent chromium (164.62 mg g−1). Thermodynamic studies reveal that the adsorption process is spontaneous and endothermic, with increased efficiency at higher temperatures, indicating suitability across various thermal conditions. MAST achieves rapid equilibrium within 20 minutes, conforms to pseudo-second-order and Langmuir models, and exhibits selective adsorption in complex matrices. These attributes underscore its potential for broad environmental remediation applications. Furthermore, MAST can be easily separated from water using magnets and retains 60 % of its effectiveness after five usage cycles, endorsing its feasibility for repeated use

Myricetin antagonizes semen-derived enhancer of viral infection (SEVI) formation and influences its infection-enhancing activity

Abstract Background Semen is a critical vector for human immunodeficiency virus (HIV) sexual transmission and harbors seminal amyloid fibrils that can markedly enhance HIV infection. Semen-derived enhancer of viral infection (SEVI) is one of the best-characterized seminal amyloid fibrils. Due to their highly cationic properties, SEVI fibrils can capture HIV virions, increase viral attachment to target cells, and augment viral fusion. Some studies have reported that myricetin antagonizes amyloid β-protein (Aβ) formation; myricetin also displays strong anti-HIV activity in vitro. Results Here, we report that myricetin inhibits the formation of SEVI fibrils by binding to the amyloidogenic region of the SEVI precursor peptide (PAP248–286) and disrupting PAP248–286 oligomerization. In addition, myricetin was found to remodel preformed SEVI fibrils and to influence the activity of SEVI in promoting HIV-1 infection. Moreover, myricetin showed synergistic effects against HIV-1 infection in combination with other antiretroviral drugs in semen. Conclusions Incorporation of myricetin into a combination bifunctional microbicide with both anti-SEVI and anti-HIV activities is a highly promising approach to preventing sexual transmission of HIV

MOESM1 of Myricetin antagonizes semen-derived enhancer of viral infection (SEVI) formation and influences its infection-enhancing activity

Additional file 1: Figure S1. Myricetin inhibits other seminal amyloid fibril formation, as shown by ThT assays. (a) SEM186-107; (b) SEM286-107. Peptide (3 mg/ml) was incubated with myricetin (200, 100, 50 and 10 μg/ml) and agitated at 1,400 rpm at 37 °C. Then samples were collected and monitored by ThT. Average values (± SD) were calculated from triplicate measurements, and the data represent one representative trial of three independent experiment. Figure S2. Amyloid fibril samples display loss of enhancement of HIV-1 infection in the presence of myricetin. The raw luciferase activities of mixed SEVI fibril samples prepared in the presence or absence of myricetin with HIV-1SF162 (a) and HIV-1NL4-3 (b) infectious clones. The values shown here represent the mean ± SD (n = 3). One-way ANOVA with Dunnett’s post hoc multiple comparisons test was used to statistically analyze the differences between samples containing PAP248-286 alone and samples containing PAP248-286 and myricetin (*p < 0.05; **p < 0.01, ***p < 0.001). Figure S3. SEVI (50 μg/ml) was incubated with myricetin at various concentrations (50, 25, 12.5, 6.25, 3.13, 1.56, 0.78 and 0.39 μg/ml). The mixtures were washed one to five times with PBS buffer and centrifuged to remove soluble myricetin. The pellets were resuspended in the original volume of medium and mixed with CCR5-tropic HIV-1SF162 (a) or CXCR4-tropic HIV-1NL4-3 (b). The luciferase activities of the cultures were measured at 72 h post-infection. Average values (± SD) were calculated from triplicate measurements; the data shown here represent one representative trial of three independent experiments. One-way ANOVA with Dunnett’s post hoc multiple comparisons test was used to statistically analyze the differences between samples containing SEVI alone and samples containing SEVI and myricetin (*p < 0.05; **p < 0.01, ***p < 0.001). Figure S4. The total p24 antigens of the mixtures of myricetin at various concentrations and 100 ng/ml HIV-1 virions without SEVI fibrils were detected in parallel with virus pull-down assays under the exact same conditions. (a) HIV-1SF162 and (b) HIV-1NL4-3. Average values (± SD) were calculated from triplicate measurements, and the data represent one representative trial of three independent experiment