Shear-induced amyloid fibrillization

The role of inertia

Samantha A. McBride, Sean P. Sanford, Juan Lopez, Amir H. Hirsa

Research output: Contribution to journalArticle

10 Citations (Scopus)

Abstract

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.

Original languageEnglish (US)
Pages (from-to)3461-3467
Number of pages7
JournalSoft Matter
Volume12
Issue number14
DOIs
StatePublished - Apr 14 2016

Fingerprint

Amyloid
inertia
shear
proteins
agitation
Proteins
insulin
Advection
advection
shearing
Shearing
Seed
seeds
fragmentation
Agglomeration
alignment
Insulin
Kinetics
Fluids
fluids

ASJC Scopus subject areas

  • Chemistry(all)
  • Condensed Matter Physics

Cite this

McBride, S. A., Sanford, S. P., Lopez, J., & Hirsa, A. H. (2016). Shear-induced amyloid fibrillization: The role of inertia. Soft Matter, 12(14), 3461-3467. https://doi.org/10.1039/c5sm02916c

Shear-induced amyloid fibrillization : The role of inertia. / McBride, Samantha A.; Sanford, Sean P.; Lopez, Juan; Hirsa, Amir H.

In: Soft Matter, Vol. 12, No. 14, 14.04.2016, p. 3461-3467.

Research output: Contribution to journalArticle

McBride, SA, Sanford, SP, Lopez, J & Hirsa, AH 2016, 'Shear-induced amyloid fibrillization: The role of inertia', Soft Matter, vol. 12, no. 14, pp. 3461-3467. https://doi.org/10.1039/c5sm02916c
McBride, Samantha A. ; Sanford, Sean P. ; Lopez, Juan ; Hirsa, Amir H. / Shear-induced amyloid fibrillization : The role of inertia. In: Soft Matter. 2016 ; Vol. 12, No. 14. pp. 3461-3467.
@article{0006f28fbb5e42198d9b4a6a22b75294,
title = "Shear-induced amyloid fibrillization: The role of inertia",
abstract = "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.",
author = "McBride, {Samantha A.} and Sanford, {Sean P.} and Juan Lopez and Hirsa, {Amir H.}",
year = "2016",
month = "4",
day = "14",
doi = "10.1039/c5sm02916c",
language = "English (US)",
volume = "12",
pages = "3461--3467",
journal = "Soft Matter",
issn = "1744-683X",
publisher = "Royal Society of Chemistry",
number = "14",

}

TY - JOUR

T1 - Shear-induced amyloid fibrillization

T2 - The role of inertia

AU - McBride, Samantha A.

AU - Sanford, Sean P.

AU - Lopez, Juan

AU - Hirsa, Amir H.

PY - 2016/4/14

Y1 - 2016/4/14

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=84962383000&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84962383000&partnerID=8YFLogxK

U2 - 10.1039/c5sm02916c

DO - 10.1039/c5sm02916c

M3 - Article

VL - 12

SP - 3461

EP - 3467

JO - Soft Matter

JF - Soft Matter

SN - 1744-683X

IS - 14

ER -