Effects of curcumin and ferulic acid on the folding of amyloid‐β peptide

Abstract

The polyphenols curcumin (CU) and ferulic acid (FA) are able to inhibit the aggregation of amyloid‐β (Aβ) peptide with different strengths. CU is a strong inhibitor while FA is a weaker one. In the present study, we examine the effects of CU and FA on the folding process of an Aβ monomer by 1 μs molecular dynamics (MD) simulations. We found that both inhibitors increase the helical propensity and decrease the non‐helical propensity of Aβ peptide. They prevent the formation of a dense bulk core and shorten the average lifetime of intramolecular hydrogen bonds in Aβ. CU makes more and longer‐lived hydrogen bonds, hydrophobic, π–π, and cation–π interactions with Aβ peptide than FA does, which is in a good agreement with the observed stronger in-hibitory activity of CU on Aβ aggregation.