Linalool acts as a chemical chaperone by inhibiting amyloid-β aggregation
Article
Singh, R, Kaur, N, Dhingra, N et al. (2024). Linalool acts as a chemical chaperone by inhibiting amyloid-β aggregation
. NEUROCHEMISTRY INTERNATIONAL, 177 10.1016/j.neuint.2024.105762
Singh, R, Kaur, N, Dhingra, N et al. (2024). Linalool acts as a chemical chaperone by inhibiting amyloid-β aggregation
. NEUROCHEMISTRY INTERNATIONAL, 177 10.1016/j.neuint.2024.105762
Linalool is a neuroprotective monoterpene found in essential oils from aromatic plants. Linalool's effectiveness in AD animal models has been established previously, but its mechanisms of action remain unclear. Therefore, this study aims to investigate whether linalool binds directly to the amyloid beta (Aβ) fibrils to understand it's role in preventing neurodegeneration. The anti-aggregation ability of Linalool was determined using Dithiothreitol (DTT), and thermal aggregation assays followed by Thioflavin T (ThT) binding assay. AD animals were treated with Linalool, and Thioflavin T staining was used to check the binding of linalool to Aβ fibrils in rat brain tissue sections. Preliminary studies revealed the anti-aggregation potential of linalool under the thermal and chemical stimulus. Further, in ThT binding assay Linalool inhibited Aβ aggregation, binding directly to Aβ fibrils. The reduced fluorescence intensity of ThT in AD brain tissues following linalool administration, highlights its neuroprotective potential as a therapeutic agent for AD.