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  • Α-mangostin, a polyphenolic xanthone derivative from mangosteen, attenuates β-amyloid oligomers-induced neurotoxicity by inhibiting amyloid aggregation.

Α-mangostin, a polyphenolic xanthone derivative from mangosteen, attenuates β-amyloid oligomers-induced neurotoxicity by inhibiting amyloid aggregation.

Neuropharmacology (2011-10-01)
Yan Wang, Zheng Xia, Jian-Rong Xu, Yan-Xia Wang, Li-Na Hou, Yu Qiu, Hong-Zhuan Chen
RESUMEN

Alzheimer's disease (AD) is a progressive neurodegenerative disease characterized by the accumulation of β-sheet-rich amyloid oligomers or fibrils which are associated with cellular toxicity in the brain. Inhibition of Aβ aggregation could be a viable therapeutic strategy for slowing and/or preventing the progress of AD. Here we reported that α-mangostin (α-M), a polyphenolic xanthone derivative from mangosteen, concentration-dependently attenuated the neurotoxicity induced by Aβ-(1-40) or Aβ-(1-42) oligomers (EC(50) = 3.89 nM, 4.14 nM respectively) as observed by decreased cell viability and impaired neurite outgrowth in primary rat cerebral cortical neurons. Molecular docking and dynamics simulations demonstrated that α-M could potentially bind to Aβ and stabilize α-helical conformation. α-M was found to directly dissociate Aβ-(1-40) and Aβ-(1-42) oligomers by blotting with oligomer-specific antibodies. ThioflavinT fluorescence assay and electron microscopy imaging further demonstrated that α-M blocked the fibril formation as well as disturbed the pre-formed fibrils. Taken together, our results indicate that α-M is capable to inhibit and dissociate the Aβ aggregation, which could contribute to its effect of attenuating Aβ oligomers-induced neurotoxicity. Thus, α-M could be a great potential candidate for AD treatment. This article is part of a Special Issue entitled 'Post-Traumatic Stress Disorder'.

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Sigma-Aldrich
α-Mangostin, ≥98% (HPLC)
Sigma-Aldrich
Amyloid β 1-42 rat, ≥90% (HPLC)
Sigma-Aldrich
Amyloid β 1-40 rat, ≥95% (HPLC)
Sigma-Aldrich
Amyloid β 1-16 rat

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