Evaluation of the Inhibitory Potential of Platinum(II) Curcumin Complex on Aβ (1–42) Peptide Aggregation: Insights from Simulation at 310 K

Abstract 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 techniques, 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 platinum(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.