Cargando…

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...

Descripción completa

Detalles Bibliográficos
Autores principales: Huang, Shu-Hsiang, Ke, Shyue-Chu, Lin, Ta-Hsin, Huang, Hsin-Bin, Chen, Yi-Cheng
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2014
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
_version_ 1782305824600752128
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
work_keys_str_mv AT huangshuhsiang effectofcterminalresiduesofaboncopperbindingaffinitystructuralconversionandaggregation
AT keshyuechu effectofcterminalresiduesofaboncopperbindingaffinitystructuralconversionandaggregation
AT lintahsin effectofcterminalresiduesofaboncopperbindingaffinitystructuralconversionandaggregation
AT huanghsinbin effectofcterminalresiduesofaboncopperbindingaffinitystructuralconversionandaggregation
AT chenyicheng effectofcterminalresiduesofaboncopperbindingaffinitystructuralconversionandaggregation