Journal
JOURNAL OF PHYSICS-CONDENSED MATTER
Volume 25, Issue 37, Pages -Publisher
IOP PUBLISHING LTD
DOI: 10.1088/0953-8984/25/37/373101
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Funding
- Engineering and Physical Sciences Research Council [EPSRC EP/J007404/1]
- Biotechnology and Biological Sciences Research Council [BBSRC BB/H013636/1]
- BBSRC [BB/H013636/1] Funding Source: UKRI
- EPSRC [EP/J007404/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/H013636/1] Funding Source: researchfish
- Engineering and Physical Sciences Research Council [EP/J007404/1] Funding Source: researchfish
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Amyloid and amyloid-like fibrils are self-assembling protein nanostructures, of interest for their robust material properties and inherent biological compatibility as well as their putative role in a number of debilitating mammalian disorders. Understanding fibril formation is essential to the development of strategies to control, manipulate or prevent fibril growth. As such, this area of research has attracted significant attention over the last half century. This review describes a number of different models that have been formulated to describe the kinetics of fibril assembly. We describe the macroscopic implications of mechanisms in which secondary processes such as secondary nucleation, fragmentation or branching dominate the assembly pathway, compared to mechanisms dominated by the influence of primary nucleation. We further describe how experimental data can be analysed with respect to the predictions of kinetic models.
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