Issue 2, 2012
From the journal:

Soft Matter

Bovine serum albumin unfolds in Couette flow†

Innocent B. Bekard,a   Peter Asimakis,a   Chai L. Teoh,bc   Tim Ryan,bc   Geoffrey J. Howlett,bc   Joseph Bertolinid  and  Dave E. Dunstan*a  

* Corresponding authors

a Department of Chemical and Biomolecular Engineering, The University of Melbourne, Victoria, Australia
E-mail: davided@unimelb.edu.au

b Department of Biochemistry and Molecular Biology, The University of Melbourne, Victoria, Australia

c Bio21 Molecular Science and Biotechnology Institute, The University of Melbourne, Victoria, Australia

d Research and Development Department, CSL Bioplasma, Broadmeadows, Victoria, Australia

Abstract

Direct measurements of the effect of hydrodynamic forces generated in Couette flow on the secondary and tertiary structure of bovine serum albumin (BSA) are reported. Real time measurements were made using both fluorescence and circular dichroism spectroscopy as complementary measures of protein structure. Our results demonstrate that BSA, a medium sized, predominantly α-helical protein, unfolds irreversibly in simple shear flow. The shear rates used in this study are comparable to those encountered in bioprocessing and in physiology. Flow-induced unfolding of BSA occurs in simple Couette flow where both exposure time and shear rate increase the degree of irreversible unfolding.

Graphical abstract: Bovine serum albumin unfolds in Couette flow

About
Cited by
Related
Download options Please wait...

Supplementary files

Article information

DOI
https://doi.org/10.1039/C1SM06704D
Article type
Paper
Submitted
09 Sep 2011
Accepted
28 Sep 2011
First published
26 Oct 2011

Soft Matter, 2012,8, 385-389

Permissions

Request permissions

Bovine serum albumin unfolds in Couette flow

I. B. Bekard, P. Asimakis, C. L. Teoh, T. Ryan, G. J. Howlett, J. Bertolini and D. E. Dunstan, Soft Matter, 2012, 8, 385 DOI: 10.1039/C1SM06704D

To request permission to reproduce material from this article, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.

Social activity

Spotlight

Advertisements