Protein Fibrillation under Crowded Conditions
Protein amyloid fibrils have widespread implications for human health. Over the last twenty years, fibrillation has been studied using a variety of crowding agents to mimic the packed interior of cells or to probe the mechanisms and pathways of the process. We tabulate and review these results by co...
| Main Authors: | , , |
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| Format: | Article |
| Language: | English |
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MDPI AG
2022-07-01
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| Series: | Biomolecules |
| Subjects: | |
| Online Access: | https://www.mdpi.com/2218-273X/12/7/950 |
| _version_ | 1827597831519600640 |
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| author | Annelise H. Gorensek-Benitez Bryan Kirk Jeffrey K. Myers |
| author_facet | Annelise H. Gorensek-Benitez Bryan Kirk Jeffrey K. Myers |
| author_sort | Annelise H. Gorensek-Benitez |
| collection | DOAJ |
| description | Protein amyloid fibrils have widespread implications for human health. Over the last twenty years, fibrillation has been studied using a variety of crowding agents to mimic the packed interior of cells or to probe the mechanisms and pathways of the process. We tabulate and review these results by considering three classes of crowding agent: synthetic polymers, osmolytes and other small molecules, and globular proteins. While some patterns are observable for certain crowding agents, the results are highly variable and often depend on the specific pairing of crowder and fibrillating protein. |
| first_indexed | 2024-03-09T03:39:53Z |
| format | Article |
| id | doaj.art-e867f5cd2c5e41f5bcf7d0e3ce66d654 |
| institution | Directory Open Access Journal |
| issn | 2218-273X |
| language | English |
| last_indexed | 2024-03-09T03:39:53Z |
| publishDate | 2022-07-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Biomolecules |
| spelling | doaj.art-e867f5cd2c5e41f5bcf7d0e3ce66d6542023-12-03T14:43:33ZengMDPI AGBiomolecules2218-273X2022-07-0112795010.3390/biom12070950Protein Fibrillation under Crowded ConditionsAnnelise H. Gorensek-Benitez0Bryan Kirk1Jeffrey K. Myers2Department of Chemistry and Biochemistry, Colorado College, Colorado Springs, CO 80903, USADepartment of Biology, Davidson College, Davidson, NC 28035, USADepartment of Chemistry, Davidson College, Davidson, NC 28035, USAProtein amyloid fibrils have widespread implications for human health. Over the last twenty years, fibrillation has been studied using a variety of crowding agents to mimic the packed interior of cells or to probe the mechanisms and pathways of the process. We tabulate and review these results by considering three classes of crowding agent: synthetic polymers, osmolytes and other small molecules, and globular proteins. While some patterns are observable for certain crowding agents, the results are highly variable and often depend on the specific pairing of crowder and fibrillating protein.https://www.mdpi.com/2218-273X/12/7/950aggregationamyloid fibrilexcluded volumemolecular crowdingneurodegenerative diseasemolecular crowding |
| spellingShingle | Annelise H. Gorensek-Benitez Bryan Kirk Jeffrey K. Myers Protein Fibrillation under Crowded Conditions Biomolecules aggregation amyloid fibril excluded volume molecular crowding neurodegenerative disease molecular crowding |
| title | Protein Fibrillation under Crowded Conditions |
| title_full | Protein Fibrillation under Crowded Conditions |
| title_fullStr | Protein Fibrillation under Crowded Conditions |
| title_full_unstemmed | Protein Fibrillation under Crowded Conditions |
| title_short | Protein Fibrillation under Crowded Conditions |
| title_sort | protein fibrillation under crowded conditions |
| topic | aggregation amyloid fibril excluded volume molecular crowding neurodegenerative disease molecular crowding |
| url | https://www.mdpi.com/2218-273X/12/7/950 |
| work_keys_str_mv | AT annelisehgorensekbenitez proteinfibrillationundercrowdedconditions AT bryankirk proteinfibrillationundercrowdedconditions AT jeffreykmyers proteinfibrillationundercrowdedconditions |