Journal
BIOMOLECULES
Volume 12, Issue 7, Pages -Publisher
MDPI
DOI: 10.3390/biom12070950
Keywords
aggregation; amyloid fibril; excluded volume; molecular crowding; neurodegenerative disease; molecular crowding; osmolyte; polyol; protein fibrillation; proteopathy; synthetic polymer; viscosity
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Funding
- Faculty Study and Research Grant from Davidson College and a Curriculum Development Grant from the Dean of the Faculty at Colorado College
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Protein amyloid fibrils have significant implications for human health. The study of fibrillation involves the use of various crowding agents to mimic cellular environments, and the results vary depending on the specific pairing of crowder and fibrillating protein.
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.
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