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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2021-05-01
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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 |
work_keys_str_mv |
AT evdokiyasalamanova effectsofcurcuminandferulicacidonthefoldingofamyloidbpeptide AT mariyanaatanasova effectsofcurcuminandferulicacidonthefoldingofamyloidbpeptide AT ivandimitrov effectsofcurcuminandferulicacidonthefoldingofamyloidbpeptide AT irinidoytchinova effectsofcurcuminandferulicacidonthefoldingofamyloidbpeptide |
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1721417149154590720 |