Modelling amyloid fibril formation kinetics: mechanisms of nucleation and growth

J E Gillam, C E MacPhee

Research output: Contribution to journalArticlepeer-review

Abstract

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.
Original languageEnglish
Pages (from-to)373101
JournalJournal of Physics: Condensed Matter
Volume25
Issue number37
DOIs
Publication statusPublished - 18 Sep 2013

Fingerprint

Dive into the research topics of 'Modelling amyloid fibril formation kinetics: mechanisms of nucleation and growth'. Together they form a unique fingerprint.

Cite this