The effect of curcumin on the stability of Aβ dimers
Aβ oligomers are potential targets for the diagnosis and therapy of Alzheimer’s disease (AD). On the other hand, the molecule curcumin has been shown to possess significant therapeutic potential in many areas. In this paper, we use all-atom explicit solvent molecular dynamics simulations to study th...
| Main Authors: | , , , , |
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| Format: | Journal Article |
| Language: | English |
| Published: |
2013
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| Online Access: | https://hdl.handle.net/10356/98827 http://hdl.handle.net/10220/17215 |
| _version_ | 1826124191021137920 |
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| author | Zhao, Li Na Chiu, See-Wing Benoit, Jérôme Chew, Lock Yue Mu, Yuguang |
| author2 | School of Biological Sciences |
| author_facet | School of Biological Sciences Zhao, Li Na Chiu, See-Wing Benoit, Jérôme Chew, Lock Yue Mu, Yuguang |
| author_sort | Zhao, Li Na |
| collection | NTU |
| description | Aβ oligomers are potential targets for the diagnosis and therapy of Alzheimer’s disease (AD). On the other hand, the molecule curcumin has been shown to possess significant therapeutic potential in many areas. In this paper, we use all-atom explicit solvent molecular dynamics simulations to study the effect of curcumin on the stability of Aβ amyloid protein oligomers. We observed that curcumin decreases the β-sheet secondary structural content within the Aβ oligomers without reducing the contacts between the monomers. The breaking of the β-sheet is found to be preceded by a deformation of the β-sheet structure due to hydrophobic interaction from the nearby curcumin. Furthermore, the π-stacking interaction between curcumin (keto ring and enol ring) and the aromatic residues of Aβ, which exists throughout the simulations, has also contributed to the diminishing of the β-sheet structure. Our analysis of the underwrapped amide–carbonyl hydrogen bonds reveals several stable dehydrons of the oligomer, especially the dehydron pair 34L and 41I, which curcumin tends to hover over. We have examined the paths of curcumin on the Aβ proteins and determined the common routes where curcumin lingers as it traverses around the Aβ. In consequence, our study has provided a detailed interaction picture between curcumin and the Aβ oligomers. |
| first_indexed | 2024-10-01T06:16:37Z |
| format | Journal Article |
| id | ntu-10356/98827 |
| institution | Nanyang Technological University |
| language | English |
| last_indexed | 2024-10-01T06:16:37Z |
| publishDate | 2013 |
| record_format | dspace |
| spelling | ntu-10356/988272020-03-07T12:34:41Z The effect of curcumin on the stability of Aβ dimers Zhao, Li Na Chiu, See-Wing Benoit, Jérôme Chew, Lock Yue Mu, Yuguang School of Biological Sciences School of Physical and Mathematical Sciences DRNTU::Science::Chemistry::Analytical chemistry::Proteins Aβ oligomers are potential targets for the diagnosis and therapy of Alzheimer’s disease (AD). On the other hand, the molecule curcumin has been shown to possess significant therapeutic potential in many areas. In this paper, we use all-atom explicit solvent molecular dynamics simulations to study the effect of curcumin on the stability of Aβ amyloid protein oligomers. We observed that curcumin decreases the β-sheet secondary structural content within the Aβ oligomers without reducing the contacts between the monomers. The breaking of the β-sheet is found to be preceded by a deformation of the β-sheet structure due to hydrophobic interaction from the nearby curcumin. Furthermore, the π-stacking interaction between curcumin (keto ring and enol ring) and the aromatic residues of Aβ, which exists throughout the simulations, has also contributed to the diminishing of the β-sheet structure. Our analysis of the underwrapped amide–carbonyl hydrogen bonds reveals several stable dehydrons of the oligomer, especially the dehydron pair 34L and 41I, which curcumin tends to hover over. We have examined the paths of curcumin on the Aβ proteins and determined the common routes where curcumin lingers as it traverses around the Aβ. In consequence, our study has provided a detailed interaction picture between curcumin and the Aβ oligomers. 2013-11-01T06:03:19Z 2019-12-06T20:00:02Z 2013-11-01T06:03:19Z 2019-12-06T20:00:02Z 2012 2012 Journal Article Zhao, L. N., Chiu, S.-W., Benoit, J., Chew, L. Y., & Mu, Y. (2012). The effect of curcumin on the stability of Aβ dimers. The Journal of Physical Chemistry B, 116(25), 7428-7435. https://hdl.handle.net/10356/98827 http://hdl.handle.net/10220/17215 10.1021/jp3034209 en The journal of physical chemistry B |
| spellingShingle | DRNTU::Science::Chemistry::Analytical chemistry::Proteins Zhao, Li Na Chiu, See-Wing Benoit, Jérôme Chew, Lock Yue Mu, Yuguang The effect of curcumin on the stability of Aβ dimers |
| title | The effect of curcumin on the stability of Aβ dimers |
| title_full | The effect of curcumin on the stability of Aβ dimers |
| title_fullStr | The effect of curcumin on the stability of Aβ dimers |
| title_full_unstemmed | The effect of curcumin on the stability of Aβ dimers |
| title_short | The effect of curcumin on the stability of Aβ dimers |
| title_sort | effect of curcumin on the stability of aβ dimers |
| topic | DRNTU::Science::Chemistry::Analytical chemistry::Proteins |
| url | https://hdl.handle.net/10356/98827 http://hdl.handle.net/10220/17215 |
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