RESUMEN
Researchers have concentrated efforts in the search for natural-based reversible inhibitors for cholinesterase enzymes as they may play a key role in the treatment of degenerative diseases. Diverse plant alkaloids can inhibit the action of acetylcholinesterase and, among them, berberine is a promising bioactive. However, berberine has poor water solubility and low bioavailability, which makes it difficult to use in treatment. The solid dispersion technique can improve the water affinity of hydrophobic substances, but berberine solid dispersions have not been extensively studied. Safety testing is also essential to ensure that the berberine-loaded solid dispersions are safe for use. This study investigated the effectiveness of berberine-loaded solid dispersions (SD) as inhibitors of acetylcholinesterase enzyme (AChE). Docking simulation was used to investigate the influence of berberine on AChE, and in vitro assays were conducted to confirm the enzymatic kinetics of AChE in the presence of berberine. Berberine SD also showed improved cytotoxic effects on tumoral cells when dispersed in aqueous media. In vivo assays using Allium cepa were implemented, and no cytotoxicity/genotoxicity was found for the berberine solid dispersion. These results suggest that berberine SD could be a significant step towards safe nanostructures for use in the treatment of neurodegenerative diseases.
Asunto(s)
Alcaloides , Berberina , Nanopartículas , Berberina/farmacología , Berberina/química , Acetilcolinesterasa , AguaRESUMEN
The use of laccases applied in bioremediation processes has been increasingly studied, given the urgent need to overcome the environmental problems caused by emerging contaminants. It is known that immobilized enzymes have better operational stability under reaction conditions, allowing for greater applicability. However, given the lack of commercially available immobilized laccases, the search for immobilization materials and methods continues to gain effort. The use of polyacrylonitrile (PAN) to immobilize enzymes has been investigated since it is a low-cost material and can be modified and functionalized to well interact with the enzyme. This polymer can be used with different morphologies such as fibers, beads, and core-shell, presenting as an easily applicable alternative. This review presents the missing link between polymer and enzyme through an overview of PAN's current use as support for laccase immobilization and polymer functionalization methods, considering the importance of immobilized laccases in several industrial sectors.