PeerJ | |
Exploring the potential of deep-blue autofluorescence for monitoring amyloid fibril formation and dissociation | |
article | |
Mantas Ziaunys1  Tomas Sneideris1  Vytautas Smirnovas1  | |
[1] Vilnius University, Life Sciences Center, Institute of Biotechnology | |
关键词: Amyloid; Deep-blue autofluorescence; Insulin; Lysozyme; Prion protein; Aggregation kinetics; Fibril dissociation; | |
DOI : 10.7717/peerj.7554 | |
学科分类:社会科学、人文和艺术(综合) | |
来源: Inra | |
【 摘 要 】
Protein aggregation into amyloid fibrils has been linked to multiple neurodegenerative disorders. Determining the kinetics of fibril formation, as well as their structural stability are important for the mechanistic understanding of amyloid aggregation. Tracking both fibril association and dissociation is usually performed by measuring light scattering of the solution or fluorescence of amyloid specific dyes, such as thioflavin-T. A possible addition to these methods is the recently discovered deep-blue autofluorescence (dbAF), which is linked to amyloid formation. In this work we explore the potential of this phenomenon to monitor amyloid fibril formation and dissociation, as well as show its possible relation to fibril size rather than amyloid structure.
【 授权许可】
CC BY
【 预 览 】
Files | Size | Format | View |
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RO202307100009885ZK.pdf | 5751KB | download |