Taylor dispersion analysis and release studies of β-carotene-loaded PLGA nanoparticles and liposomes in simulated gastrointestinal fluids.

β-Carotene (βC), a natural carotenoid, is the most important and effective vitamin A precursor, known also for its antioxidant properties. However, its poor water solubility, chemical instability, and low bioavailability limit its effectiveness as an orally delivered functional nutrient. Nanoparticle encapsulation improves βC's bioaccessibility by enhancing its stability and solubility.

Atomically precise surface chemistry of zirconium and hafnium metal oxo clusters beyond carboxylate ligands.

The effectiveness of nanocrystals in many applications depends on their surface chemistry. Here, we leverage the atomically precise nature of zirconium and hafnium oxo clusters to gain fundamental insight into the thermodynamics of ligand binding. Through a combination of theoretical calculations and experimental spectroscopic techniques, we determine the interaction between the MO (M = Zr, Hf) cluster surface and various ligands: carboxylates, phosphonates, dialkylphosphinates, and monosubstituted phosphinates.

The impact of macrophage phenotype and heterogeneity on the total internalized gold nanoparticle counts.

Macrophages play a pivotal role in the internalization and processing of administered nanoparticles (NPs). Furthermore, the phagocytic capacity and immunological properties of macrophages can vary depending on their microenvironment, exhibiting a spectrum of polarization states ranging from pro-inflammatory M1 to anti-inflammatory M2. However, previous research investigating this phenotype-dependent interaction with NPs has predominantly relied on semi-quantitative techniques or conventional metrics to assess intracellular NPs.

Fluorescence-Based Monitoring of Early-Stage Aggregation of Amyloid-β, Amylin Peptide, Tau, and α-Synuclein Proteins.

Early-stage aggregates of amyloid-forming proteins, specifically soluble oligomers, are implicated in neurodegenerative diseases such as Alzheimer's disease, Parkinson's disease, and Huntington's disease. Protein aggregation is typically monitored by fluorescence using the amyloid-binding fluorophore thioflavin T (ThT). Thioflavin T interacts, however, preferentially with fibrillar amyloid structures rather than with soluble, early-stage aggregates.