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Effect of C-Terminal Residues of Aβ on Copper Binding Affinity, Structural Conversion and Aggregation
Many properties of Aβ such as toxicity, aggregation and ROS formation are modulated by Cu(2+). Previously, the coordination configuration and interaction of Cu(2+) with the Aβ N-terminus has been extensively studied. However, the effect of Aβ C-terminal residues on related properties is still unclea...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2014
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3940864/ https://www.ncbi.nlm.nih.gov/pubmed/24594588 http://dx.doi.org/10.1371/journal.pone.0090385 |
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author | Huang, Shu-Hsiang Ke, Shyue-Chu Lin, Ta-Hsin Huang, Hsin-Bin Chen, Yi-Cheng |
author_facet | Huang, Shu-Hsiang Ke, Shyue-Chu Lin, Ta-Hsin Huang, Hsin-Bin Chen, Yi-Cheng |
author_sort | Huang, Shu-Hsiang |
collection | PubMed |
description | Many properties of Aβ such as toxicity, aggregation and ROS formation are modulated by Cu(2+). Previously, the coordination configuration and interaction of Cu(2+) with the Aβ N-terminus has been extensively studied. However, the effect of Aβ C-terminal residues on related properties is still unclear. In the present study, several C-terminus-truncated Aβ peptides, including Aβ1-40, Aβ1-35, Aβ1-29, Aβ1-24 and Aβ1-16, were synthesized to characterize the effect of Aβ C-terminal residues on Cu(2+) binding affinity, structure, aggregation ability and ROS formation. Results show that the Aβ C-terminal residues have effect on Cu(2+) binding affinity, aggregation ability and inhibitory ability of ROS formation. Compared to the key residues responsible for Aβ aggregation and structure in the absence of Cu(2+), it is more likely that residues 36–40, rather than residues 17–21 and 30–35, play a key role on the related properties of Aβ in the presence of Cu(2+). |
format | Online Article Text |
id | pubmed-3940864 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-39408642014-03-06 Effect of C-Terminal Residues of Aβ on Copper Binding Affinity, Structural Conversion and Aggregation Huang, Shu-Hsiang Ke, Shyue-Chu Lin, Ta-Hsin Huang, Hsin-Bin Chen, Yi-Cheng PLoS One Research Article Many properties of Aβ such as toxicity, aggregation and ROS formation are modulated by Cu(2+). Previously, the coordination configuration and interaction of Cu(2+) with the Aβ N-terminus has been extensively studied. However, the effect of Aβ C-terminal residues on related properties is still unclear. In the present study, several C-terminus-truncated Aβ peptides, including Aβ1-40, Aβ1-35, Aβ1-29, Aβ1-24 and Aβ1-16, were synthesized to characterize the effect of Aβ C-terminal residues on Cu(2+) binding affinity, structure, aggregation ability and ROS formation. Results show that the Aβ C-terminal residues have effect on Cu(2+) binding affinity, aggregation ability and inhibitory ability of ROS formation. Compared to the key residues responsible for Aβ aggregation and structure in the absence of Cu(2+), it is more likely that residues 36–40, rather than residues 17–21 and 30–35, play a key role on the related properties of Aβ in the presence of Cu(2+). Public Library of Science 2014-03-03 /pmc/articles/PMC3940864/ /pubmed/24594588 http://dx.doi.org/10.1371/journal.pone.0090385 Text en © 2014 Huang et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited. |
spellingShingle | Research Article Huang, Shu-Hsiang Ke, Shyue-Chu Lin, Ta-Hsin Huang, Hsin-Bin Chen, Yi-Cheng Effect of C-Terminal Residues of Aβ on Copper Binding Affinity, Structural Conversion and Aggregation |
title | Effect of C-Terminal Residues of Aβ on Copper Binding Affinity, Structural Conversion and Aggregation |
title_full | Effect of C-Terminal Residues of Aβ on Copper Binding Affinity, Structural Conversion and Aggregation |
title_fullStr | Effect of C-Terminal Residues of Aβ on Copper Binding Affinity, Structural Conversion and Aggregation |
title_full_unstemmed | Effect of C-Terminal Residues of Aβ on Copper Binding Affinity, Structural Conversion and Aggregation |
title_short | Effect of C-Terminal Residues of Aβ on Copper Binding Affinity, Structural Conversion and Aggregation |
title_sort | effect of c-terminal residues of aβ on copper binding affinity, structural conversion and aggregation |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3940864/ https://www.ncbi.nlm.nih.gov/pubmed/24594588 http://dx.doi.org/10.1371/journal.pone.0090385 |
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