Competition between crystal and fibril formation in molecular mutations of amyloidogenic peptides
Aggregation of amyloidogenic peptides into fibrils and crystals has incidence in several amyloid-related diseases. Here, the authors investigate the origins of the fibril-to-crystal conversion in amyloidogenic hexapeptides pointing to the amyloid crystals as the ground state in the protein folding e...
| Main Authors: | , , , , , , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
Nature Portfolio
2017-11-01
|
| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/s41467-017-01424-4 |
| _version_ | 1818430614479568896 |
|---|---|
| author | Nicholas P. Reynolds Jozef Adamcik Joshua T. Berryman Stephan Handschin Ali Asghar Hakami Zanjani Wen Li Kun Liu Afang Zhang Raffaele Mezzenga |
| author_facet | Nicholas P. Reynolds Jozef Adamcik Joshua T. Berryman Stephan Handschin Ali Asghar Hakami Zanjani Wen Li Kun Liu Afang Zhang Raffaele Mezzenga |
| author_sort | Nicholas P. Reynolds |
| collection | DOAJ |
| description | Aggregation of amyloidogenic peptides into fibrils and crystals has incidence in several amyloid-related diseases. Here, the authors investigate the origins of the fibril-to-crystal conversion in amyloidogenic hexapeptides pointing to the amyloid crystals as the ground state in the protein folding energy landscape. |
| first_indexed | 2024-12-14T15:36:13Z |
| format | Article |
| id | doaj.art-f724699c0cff4d61b17cab20071aad41 |
| institution | Directory Open Access Journal |
| issn | 2041-1723 |
| language | English |
| last_indexed | 2024-12-14T15:36:13Z |
| publishDate | 2017-11-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Nature Communications |
| spelling | doaj.art-f724699c0cff4d61b17cab20071aad412022-12-21T22:55:43ZengNature PortfolioNature Communications2041-17232017-11-018111010.1038/s41467-017-01424-4Competition between crystal and fibril formation in molecular mutations of amyloidogenic peptidesNicholas P. Reynolds0Jozef Adamcik1Joshua T. Berryman2Stephan Handschin3Ali Asghar Hakami Zanjani4Wen Li5Kun Liu6Afang Zhang7Raffaele Mezzenga8Swinburne University of Technology, ARC Training Centre for Biodevices, Faculty of Science, Engineering and TechnologyETH Zurich, Department of Health Sciences & TechnologyUniversity of Luxembourg, Department of Physics and Materials ScienceETH Zurich, Department of Health Sciences & TechnologyUniversity of Luxembourg, Department of Physics and Materials ScienceShanghai University, Department of Polymer MaterialsShanghai University, Department of Polymer MaterialsShanghai University, Department of Polymer MaterialsETH Zurich, Department of Health Sciences & TechnologyAggregation of amyloidogenic peptides into fibrils and crystals has incidence in several amyloid-related diseases. Here, the authors investigate the origins of the fibril-to-crystal conversion in amyloidogenic hexapeptides pointing to the amyloid crystals as the ground state in the protein folding energy landscape.https://doi.org/10.1038/s41467-017-01424-4 |
| spellingShingle | Nicholas P. Reynolds Jozef Adamcik Joshua T. Berryman Stephan Handschin Ali Asghar Hakami Zanjani Wen Li Kun Liu Afang Zhang Raffaele Mezzenga Competition between crystal and fibril formation in molecular mutations of amyloidogenic peptides Nature Communications |
| title | Competition between crystal and fibril formation in molecular mutations of amyloidogenic peptides |
| title_full | Competition between crystal and fibril formation in molecular mutations of amyloidogenic peptides |
| title_fullStr | Competition between crystal and fibril formation in molecular mutations of amyloidogenic peptides |
| title_full_unstemmed | Competition between crystal and fibril formation in molecular mutations of amyloidogenic peptides |
| title_short | Competition between crystal and fibril formation in molecular mutations of amyloidogenic peptides |
| title_sort | competition between crystal and fibril formation in molecular mutations of amyloidogenic peptides |
| url | https://doi.org/10.1038/s41467-017-01424-4 |
| work_keys_str_mv | AT nicholaspreynolds competitionbetweencrystalandfibrilformationinmolecularmutationsofamyloidogenicpeptides AT jozefadamcik competitionbetweencrystalandfibrilformationinmolecularmutationsofamyloidogenicpeptides AT joshuatberryman competitionbetweencrystalandfibrilformationinmolecularmutationsofamyloidogenicpeptides AT stephanhandschin competitionbetweencrystalandfibrilformationinmolecularmutationsofamyloidogenicpeptides AT aliasgharhakamizanjani competitionbetweencrystalandfibrilformationinmolecularmutationsofamyloidogenicpeptides AT wenli competitionbetweencrystalandfibrilformationinmolecularmutationsofamyloidogenicpeptides AT kunliu competitionbetweencrystalandfibrilformationinmolecularmutationsofamyloidogenicpeptides AT afangzhang competitionbetweencrystalandfibrilformationinmolecularmutationsofamyloidogenicpeptides AT raffaelemezzenga competitionbetweencrystalandfibrilformationinmolecularmutationsofamyloidogenicpeptides |