Effects of Curcumin and Ferulic Acid on the Folding of Amyloid-β Peptide

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A11-positive β-amyloid Oligomer Preparation and Assessment Using Dot Blotting Analysis

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Published on: May 22, 2018

Evdokiya Salamanova¹, Mariyana Atanasova¹, Ivan Dimitrov¹

¹Faculty of Pharmacy, Medical University of Sofia, 1000 Sofia, Bulgaria.

Molecules (Basel, Switzerland)

|June 2, 2021

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 inhibitory activity of CU on Aβ aggregation.

Keywords:

amyloid-β peptide curcumin ferulic acid folding hydrogen bonding molecular dynamics simulation secondary structure solvent-accessible surface area

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