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Abstract
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Aberrant protein folding and amyloid aggregation is known as
the main mechanism of fibrillation in amyloidosis diseases such
as Alzheimer’s disease. In this study, using computational tech-
niques, we investigated the inhibitory effects of a platinum(II)
curcumin complex on Aβ aggregation. Docking calculations
showed that platinum(II) curcumin is a better binder to Aβ
oligomer than curcumin itself. The molecular dynamics (MD)
simulation was conducted to evaluate the possibility of the
destabilization effect of platinum(II) curcumin on Aβ oligomers.
The diversion of RMSD, RMSF, MSD, potential energy, and SASA
trends indicate Aβ fibril instability in the presence of plat-
inum(II) curcumin complex. The notable decline in the number
of hydrogen bonds, salt bridges, and β-sheet content results in
the conformational changes in the Aβ fibril structure and the
reduction of its neurotoxicity. We believe that our results could
help to elucidate the mechanisms of the antiaggregation effects
of platinum(II) curcumin complex and provide a ground base for
experimental antiaggregation research on this compound.
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