Self-Assembly of Amyloid Fibrils into 3D Gel Clusters versus 2D Sheets
The deposition of dense fibril plaques represents the pathological hallmark for a multitude of human disorders, including many neurodegenerative diseases. Fibril plaques are predominately composed of amyloid fibrils, characterized by their underlying cross beta-sheet architecture. Research into the...
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| Format: | Article |
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MDPI AG
2023-01-01
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| Series: | Biomolecules |
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| Online Access: | https://www.mdpi.com/2218-273X/13/2/230 |
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| author | Kanchana Karunarathne Nabila Bushra Olivia Williams Imad Raza Laura Tirado Diane Fakhre Fadia Fakhre Martin Muschol |
| author_facet | Kanchana Karunarathne Nabila Bushra Olivia Williams Imad Raza Laura Tirado Diane Fakhre Fadia Fakhre Martin Muschol |
| author_sort | Kanchana Karunarathne |
| collection | DOAJ |
| description | The deposition of dense fibril plaques represents the pathological hallmark for a multitude of human disorders, including many neurodegenerative diseases. Fibril plaques are predominately composed of amyloid fibrils, characterized by their underlying cross beta-sheet architecture. Research into the mechanisms of amyloid formation has mostly focused on characterizing and modeling the growth of individual fibrils and associated oligomers from their monomeric precursors. Much less is known about the mechanisms causing individual fibrils to assemble into ordered fibrillar suprastructures. Elucidating the mechanisms regulating this “secondary” self-assembly into distinct suprastructures is important for understanding how individual protein fibrils form the prominent macroscopic plaques observed in disease. Whether and how amyloid fibrils assemble into either 2D or 3D supramolecular structures also relates to ongoing efforts on using amyloid fibrils as substrates or scaffolds for self-assembling functional biomaterials. Here, we investigated the conditions under which preformed amyloid fibrils of a lysozyme assemble into larger superstructures as a function of charge screening or pH. Fibrils either assembled into three-dimensional gel clusters or two-dimensional fibril sheets. The latter displayed optical birefringence, diagnostic of amyloid plaques. We presume that pH and salt modulate fibril charge repulsion, which allows anisotropic fibril–fibril attraction to emerge and drive the transition from 3D to 2D fibril self-assembly. |
| first_indexed | 2024-03-11T09:05:48Z |
| format | Article |
| id | doaj.art-3eb5e53dd26a4c2abe22c79fd0ea7368 |
| institution | Directory Open Access Journal |
| issn | 2218-273X |
| language | English |
| last_indexed | 2024-03-11T09:05:48Z |
| publishDate | 2023-01-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Biomolecules |
| spelling | doaj.art-3eb5e53dd26a4c2abe22c79fd0ea73682023-11-16T19:22:12ZengMDPI AGBiomolecules2218-273X2023-01-0113223010.3390/biom13020230Self-Assembly of Amyloid Fibrils into 3D Gel Clusters versus 2D SheetsKanchana Karunarathne0Nabila Bushra1Olivia Williams2Imad Raza3Laura Tirado4Diane Fakhre5Fadia Fakhre6Martin Muschol7Department of Physics, University of South Florida, Tampa, FL 33620, USADepartment of Physics, University of South Florida, Tampa, FL 33620, USADepartment of Physics, University of South Florida, Tampa, FL 33620, USADepartment of Physics, University of South Florida, Tampa, FL 33620, USADepartment of Physics, University of South Florida, Tampa, FL 33620, USADepartment of Physics, University of South Florida, Tampa, FL 33620, USADepartment of Physics, University of South Florida, Tampa, FL 33620, USADepartment of Physics, University of South Florida, Tampa, FL 33620, USAThe deposition of dense fibril plaques represents the pathological hallmark for a multitude of human disorders, including many neurodegenerative diseases. Fibril plaques are predominately composed of amyloid fibrils, characterized by their underlying cross beta-sheet architecture. Research into the mechanisms of amyloid formation has mostly focused on characterizing and modeling the growth of individual fibrils and associated oligomers from their monomeric precursors. Much less is known about the mechanisms causing individual fibrils to assemble into ordered fibrillar suprastructures. Elucidating the mechanisms regulating this “secondary” self-assembly into distinct suprastructures is important for understanding how individual protein fibrils form the prominent macroscopic plaques observed in disease. Whether and how amyloid fibrils assemble into either 2D or 3D supramolecular structures also relates to ongoing efforts on using amyloid fibrils as substrates or scaffolds for self-assembling functional biomaterials. Here, we investigated the conditions under which preformed amyloid fibrils of a lysozyme assemble into larger superstructures as a function of charge screening or pH. Fibrils either assembled into three-dimensional gel clusters or two-dimensional fibril sheets. The latter displayed optical birefringence, diagnostic of amyloid plaques. We presume that pH and salt modulate fibril charge repulsion, which allows anisotropic fibril–fibril attraction to emerge and drive the transition from 3D to 2D fibril self-assembly.https://www.mdpi.com/2218-273X/13/2/230hen egg-white lysozymeamyloid fibrilself-assemblygelationplaque formation |
| spellingShingle | Kanchana Karunarathne Nabila Bushra Olivia Williams Imad Raza Laura Tirado Diane Fakhre Fadia Fakhre Martin Muschol Self-Assembly of Amyloid Fibrils into 3D Gel Clusters versus 2D Sheets Biomolecules hen egg-white lysozyme amyloid fibril self-assembly gelation plaque formation |
| title | Self-Assembly of Amyloid Fibrils into 3D Gel Clusters versus 2D Sheets |
| title_full | Self-Assembly of Amyloid Fibrils into 3D Gel Clusters versus 2D Sheets |
| title_fullStr | Self-Assembly of Amyloid Fibrils into 3D Gel Clusters versus 2D Sheets |
| title_full_unstemmed | Self-Assembly of Amyloid Fibrils into 3D Gel Clusters versus 2D Sheets |
| title_short | Self-Assembly of Amyloid Fibrils into 3D Gel Clusters versus 2D Sheets |
| title_sort | self assembly of amyloid fibrils into 3d gel clusters versus 2d sheets |
| topic | hen egg-white lysozyme amyloid fibril self-assembly gelation plaque formation |
| url | https://www.mdpi.com/2218-273X/13/2/230 |
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