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Andrade, Stéphanie; Pereira, Maria C.; Loureiro, Joana A.
Colloids and surfaces, B, Biointerfaces, 20/May , Letnik: 225Journal Article
Alzheimer's disease (AD) is an incurable neurological illness and the leading cause of dementia, characterized by amyloid β (Aβ) fibril deposits. Caffeic acid (CA) has demonstrated potential value for AD therapy due to its anti-amyloidogenic, anti-inflammatory, and antioxidant properties. However, its chemical instability and limited bioavailability limit its therapeutic potential in vivo. Herein, liposomes loading CA were produced by distinct techniques. Taking advantage of the overexpression of transferrin (Tf) receptors in brain endothelial cells, Tf was conjugated to the liposomes’ surface to direct the CA-loaded nanoparticles (NPs) to the blood-brain barrier (BBB). The optimized Tf-modified NPs exhibited a mean size of around 140 nm, a polydispersity index lower than 0.2, and a neutral surface charge, being appropriate for drug delivery. The Tf-functionalized liposomes showed suitable encapsulation efficiency and physical stability for at least 2 months. Furthermore, in simulated physiological settings, the NPs ensured the sustained release of CA for 8 days. The anti-amyloidogenic efficacy of the optimized drug delivery system (DDS) was investigated. The data show that CA-loaded Tf-functionalized liposomes are capable of preventing Aβ aggregation and fibril formation, and disaggregating mature fibrils. Hence, the proposed brain-targeted DDS may be a potential strategy for preventing and treating AD. Future studies in animal models of AD will be valuable to validate the therapeutic efficacy of the optimized nanosystem. Display omitted •Liposomes containing caffeic acid (CA) were produced by various techniques.•Liposomes’ surface was modified with transferrin for improved targeting ability.•Nanoparticles exhibited appropriate physicochemical properties for drug delivery.•CA-loaded liposomes inhibited the aggregation of amyloid β (Aβ) peptides.•CA-loaded liposomes disaggregated mature Aβ fibrils.
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Leto | Faktor vpliva | Izdaja | Kategorija | Razvrstitev | ||||
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JCR | SNIP | JCR | SNIP | JCR | SNIP | JCR | SNIP |
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in: SICRIS
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