L17A/F19A Substitutions Augment the α-Helicity of β-Amyloid Peptide Discordant Segment.
β-amyloid peptide (Aβ) aggregation has been thought to be associated with the pathogenesis of Alzheimer's disease. Recently, we showed that L17A/F19A substitutions may increase the structural stability of wild-type and Arctic-type Aβ40 and decrease the rates of structural conversion and fibril...
| Main Authors: | , , , , , , , |
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| Format: | Article |
| Language: | English |
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Public Library of Science (PLoS)
2016-01-01
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| Series: | PLoS ONE |
| Online Access: | http://europepmc.org/articles/PMC4841593?pdf=render |
| _version_ | 1811240735016484864 |
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| author | Chu-Ting Liang Hsien-Bin Huang Chih-Ching Wang Yi-Ru Chen Chi-Fon Chang Ming-Shi Shiao Yi-Cheng Chen Ta-Hsien Lin |
| author_facet | Chu-Ting Liang Hsien-Bin Huang Chih-Ching Wang Yi-Ru Chen Chi-Fon Chang Ming-Shi Shiao Yi-Cheng Chen Ta-Hsien Lin |
| author_sort | Chu-Ting Liang |
| collection | DOAJ |
| description | β-amyloid peptide (Aβ) aggregation has been thought to be associated with the pathogenesis of Alzheimer's disease. Recently, we showed that L17A/F19A substitutions may increase the structural stability of wild-type and Arctic-type Aβ40 and decrease the rates of structural conversion and fibril formation. However, the underlying mechanism for the increase of structural stability as a result of the alanine substitutions remained elusive. In this study, we apply nuclear magnetic resonance and circular dichroism spectroscopies to characterize the Aβ40 structure, demonstrating that L17A/F19A substitutions can augment the α-helicity of the residues located in the α/β-discordant segment (resides 15 to 23) of both wild-type and Arctic-type Aβ40. These results provide a structural basis to link the α-helicity of the α/β-discordant segment with the conformational conversion propensity of Aβ. |
| first_indexed | 2024-04-12T13:25:29Z |
| format | Article |
| id | doaj.art-b7c44c3f74f54977bae6babf14526c7f |
| institution | Directory Open Access Journal |
| issn | 1932-6203 |
| language | English |
| last_indexed | 2024-04-12T13:25:29Z |
| publishDate | 2016-01-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS ONE |
| spelling | doaj.art-b7c44c3f74f54977bae6babf14526c7f2022-12-22T03:31:21ZengPublic Library of Science (PLoS)PLoS ONE1932-62032016-01-01114e015432710.1371/journal.pone.0154327L17A/F19A Substitutions Augment the α-Helicity of β-Amyloid Peptide Discordant Segment.Chu-Ting LiangHsien-Bin HuangChih-Ching WangYi-Ru ChenChi-Fon ChangMing-Shi ShiaoYi-Cheng ChenTa-Hsien Linβ-amyloid peptide (Aβ) aggregation has been thought to be associated with the pathogenesis of Alzheimer's disease. Recently, we showed that L17A/F19A substitutions may increase the structural stability of wild-type and Arctic-type Aβ40 and decrease the rates of structural conversion and fibril formation. However, the underlying mechanism for the increase of structural stability as a result of the alanine substitutions remained elusive. In this study, we apply nuclear magnetic resonance and circular dichroism spectroscopies to characterize the Aβ40 structure, demonstrating that L17A/F19A substitutions can augment the α-helicity of the residues located in the α/β-discordant segment (resides 15 to 23) of both wild-type and Arctic-type Aβ40. These results provide a structural basis to link the α-helicity of the α/β-discordant segment with the conformational conversion propensity of Aβ.http://europepmc.org/articles/PMC4841593?pdf=render |
| spellingShingle | Chu-Ting Liang Hsien-Bin Huang Chih-Ching Wang Yi-Ru Chen Chi-Fon Chang Ming-Shi Shiao Yi-Cheng Chen Ta-Hsien Lin L17A/F19A Substitutions Augment the α-Helicity of β-Amyloid Peptide Discordant Segment. PLoS ONE |
| title | L17A/F19A Substitutions Augment the α-Helicity of β-Amyloid Peptide Discordant Segment. |
| title_full | L17A/F19A Substitutions Augment the α-Helicity of β-Amyloid Peptide Discordant Segment. |
| title_fullStr | L17A/F19A Substitutions Augment the α-Helicity of β-Amyloid Peptide Discordant Segment. |
| title_full_unstemmed | L17A/F19A Substitutions Augment the α-Helicity of β-Amyloid Peptide Discordant Segment. |
| title_short | L17A/F19A Substitutions Augment the α-Helicity of β-Amyloid Peptide Discordant Segment. |
| title_sort | l17a f19a substitutions augment the α helicity of β amyloid peptide discordant segment |
| url | http://europepmc.org/articles/PMC4841593?pdf=render |
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