Jump to main content
Jump to site search

Issue 14, 2016
Previous Article Next Article

Shear-induced amyloid fibrillization: the role of inertia

Author affiliations


Agitation of protein is known to induce deleterious effects on protein stability and structure, with extreme agitation sometimes resulting in complete aggregation into amyloid fibrils. Many mechanisms have been proposed to explain how protein becomes unstable when subjected to flow, including alignment of protein species, shear-induced unfolding, simple mixing, or fragmentation of existing fibrils to create new seeds. Here a shearing flow was imposed on a solution of monomeric human insulin via a rotating Couette device with a small hydrophobic fluid interface. The results indicate that even very low levels of shear are capable of accelerating amyloid fibril formation. Simulations of the flow suggest that the shear enhances fibrillization kinetics when flow inertia is non-negligible and the resulting meridional circulation allows for advection of bulk protein to the hydrophobic interface.

Graphical abstract: Shear-induced amyloid fibrillization: the role of inertia

Back to tab navigation

Supplementary files

Publication details

The article was received on 01 Dec 2015, accepted on 28 Feb 2016 and first published on 29 Feb 2016

Article type: Paper
DOI: 10.1039/C5SM02916C
Author version
Download author version (PDF)
Soft Matter, 2016,12, 3461-3467

  •   Request permissions

    Shear-induced amyloid fibrillization: the role of inertia

    S. A. McBride, S. P. Sanford, J. M. Lopez and A. H. Hirsa, Soft Matter, 2016, 12, 3461
    DOI: 10.1039/C5SM02916C

Search articles by author