The onset of Alzheimer's disease (AD) is associated with the presence of neurofibrillary pathology such as amyloid β (Aβ) plaques. Different therapeutic strategies have focused on the inhibition of Aβ aggregate formation; these pathological structures lead to neuronal disorder and cognitive impairment. Fullerene C₆₀ has demonstrated the ability to interact and prevent Aβ fibril development; however, its low solubility and toxicity to cells remain significant problems. In this study, we synthesized, characterized and compared diethyl fullerenemalonates and the corresponding sodium salts, adducts of C₆₀ bearing 1 to 3 diethyl malonyl and disodium malonyl substituents to evaluate the potential inhibitory effect on the aggregation of Aβ₄₂ and their biocompatibility. The dose-dependent inhibitory effect of fullerenes on Aβ₄₂ aggregation was studied using a thioflavin T fluorescent assay, and the IC₅₀ value demonstrated a low range of fullerene concentration for inhibition, as confirmed by electron microscopy. The exposure of neuroblastoma to fullerenemalonates showed low toxicity, primarily in the presence of the sodium salt-adducts. An isomeric mixture of bisadducts, trisadducts and a C₃-symetrical trisadduct demonstrated the highest efficacy among the tests. In silico calculations were performed to complement the experimental data, obtaining a deeper understanding of the Aβ inhibitory mechanism; indicating that C₃-symetrical trisadduct interacts mainly with 1D to 16K residues of Aβ₄₂ peptide. These data suggest that fullerenemalonates require specific substituents designed as sodium salt molecules to inhibit Aβ fibrillization and perform with low toxicity. These are promising molecules for developing future therapies involving Aβ aggregates in diseases such as AD and other types of dementia.

Alzheimer's disease (AD) is a progressive neurodegenerative disorder characterized by cognitive decline and memory impairments and is considered the most prevalent form of dementia. Among the contributing factors to AD lies the hyperphosphorylation of the microtubule‐associated protein tau. Phosphorylated tau reduces its affinity for microtubules and triggers other posttranslational modifications that result in its aggregation and assembly into filaments. These structures progressively accumulate within neurons leading to neurodegeneration. While current AD medications often involve undesirable side effects, the exploration of natural products as a potential therapeutic alternative has gained considerable attention. Numerous compounds have shown potential capacity for reducing tau pathology through different mechanisms, such as inhibiting kinases to reduce tau hyperphosphorylation, enhancing phosphatase activity, and blocking fibril formation. Since tau hyperphosphorylation‐induced aggregation is pivotal in AD onset, this review aims to elucidate the potential of natural products in modulating this crucial molecular mechanism.

Plaques formed by abnormal accumulation of amyloid β-peptide (Aβ) lead to onset of Alzheimer’s disease (AD). Pharmacological treatments do not reduce Aβ aggregation neither restore learning and memory. Noninvasive techniques have emerged as an alternative to treat AD, such as stimulation with electromagnetic fields (EMF) that decrease Aβ deposition and reverses cognitive impairment in AD mice, even though some studies showed side effects on parallel magnetic fields stimulation. As a new approach of magnetic field (MF) stimulation, vortex magnetic fields (VMF) have been tested inducing a random movement of charged biomolecules in cells, promoting cell viability and apparently safer than parallel magnetic fields. In this study we demonstrate the effect of VMF on Aβ aggregation. The experimental strategy includes, i) design and construction of a coil capable to induce VMF, ii) evaluation of VMF stimulation on Aβ peptide induced-fibrils-formation, iii) evaluation of VMF stimulation on SH-SY5Y neuroblastoma cell line in the presence of Aβ peptide. We demonstrated for the first time that Aβ aggregation exposed to VMF during 24 h decreased ~ 86% of Aβ fibril formation compared to control. Likewise, VMF stimulation reduced Aβ fibrils-cytotoxicity and increase SH-SY5Y cell viability. These data establish the basis for future investigation that involve VMF as inhibitor of Aβ-pathology and indicate the therapeutic potential of VMF for AD treatment.

Spondias mombin L. has been used in traditional medicine to treat some cases such as infections and inflammations. Some researchers have reported that its biological components, such as carotenoids, carotenes, and phenols, have been characterized primarily by HPLC analysis. Here, we report on the characterization of Spondias mombin L. seed oil by Raman spectroscopy, and the profile identification of fatty acids by ¹H-NMR and ¹³C-NMR spectroscopy. The oil was extracted from different weight volumes of seeds using organic solvent, and each batch was characterized. The analysis of the fatty acid profile by NMR indicated that the seed oil is highly unsaturated (monounsaturated: 29.4% and polyunsaturated: 43.5%). Molecular Raman vibrations at 1006, 1158 and 1523 cm⁻¹ showed the presence of carotenoids, which in turn performed an antioxidant activity. This was demonstrated by a 2,2′-Azino-bis (3-ethylbenzothiazoline-6-sulfonic acid) diammonium salt (ABTS) method. The cell viability in colon cancer cells was promoted in the presence of the oil. The compounds identified in this study from seed oil could be an interesting proposal for food or pharmaceutical applications.