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

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 mol...

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Main Authors: Evdokiya Salamanova, Mariyana Atanasova, Ivan Dimitrov, Irini Doytchinova
Format: Article
Language:English
Published: MDPI AG 2021-05-01
Series:Molecules
Subjects:
Online Access:https://www.mdpi.com/1420-3049/26/9/2815
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spelling doaj-32dbdc6b51144713a811fa87f8542c002021-05-31T23:35:00ZengMDPI AGMolecules1420-30492021-05-01262815281510.3390/molecules26092815Effects of Curcumin and Ferulic Acid on the Folding of Amyloid-β PeptideEvdokiya Salamanova0Mariyana Atanasova1Ivan Dimitrov2Irini Doytchinova3Faculty of Pharmacy, Medical University of Sofia, 1000 Sofia, BulgariaFaculty of Pharmacy, Medical University of Sofia, 1000 Sofia, BulgariaFaculty of Pharmacy, Medical University of Sofia, 1000 Sofia, BulgariaFaculty of Pharmacy, Medical University of Sofia, 1000 Sofia, BulgariaThe 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.https://www.mdpi.com/1420-3049/26/9/2815curcuminferulic acidamyloid-β peptidemolecular dynamics simulationfoldingsecondary structure
collection DOAJ
language English
format Article
sources DOAJ
author Evdokiya Salamanova
Mariyana Atanasova
Ivan Dimitrov
Irini Doytchinova
spellingShingle Evdokiya Salamanova
Mariyana Atanasova
Ivan Dimitrov
Irini Doytchinova
Effects of Curcumin and Ferulic Acid on the Folding of Amyloid-β Peptide
Molecules
curcumin
ferulic acid
amyloid-β peptide
molecular dynamics simulation
folding
secondary structure
author_facet Evdokiya Salamanova
Mariyana Atanasova
Ivan Dimitrov
Irini Doytchinova
author_sort Evdokiya Salamanova
title Effects of Curcumin and Ferulic Acid on the Folding of Amyloid-β Peptide
title_short Effects of Curcumin and Ferulic Acid on the Folding of Amyloid-β Peptide
title_full Effects of Curcumin and Ferulic Acid on the Folding of Amyloid-β Peptide
title_fullStr Effects of Curcumin and Ferulic Acid on the Folding of Amyloid-β Peptide
title_full_unstemmed Effects of Curcumin and Ferulic Acid on the Folding of Amyloid-β Peptide
title_sort effects of curcumin and ferulic acid on the folding of amyloid-β peptide
publisher MDPI AG
series Molecules
issn 1420-3049
publishDate 2021-05-01
description 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.
topic curcumin
ferulic acid
amyloid-β peptide
molecular dynamics simulation
folding
secondary structure
url https://www.mdpi.com/1420-3049/26/9/2815
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AT mariyanaatanasova effectsofcurcuminandferulicacidonthefoldingofamyloidbpeptide
AT ivandimitrov effectsofcurcuminandferulicacidonthefoldingofamyloidbpeptide
AT irinidoytchinova effectsofcurcuminandferulicacidonthefoldingofamyloidbpeptide
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