Bovine serum albumin unfolds in Couette flow

被引：26

作者：

Bekard, Innocent B. ^{[1
]}

Asimakis, Peter ^{[1
]}

Teoh, Chai L. ^{[2
,3
]}

Ryan, Tim ^{[2
,3
]}

Howlett, Geoffrey J. ^{[2
,3
]}

Bertolini, Joseph ^{[4
]}

Dunstan, Dave E. ^{[1
]}

机构：

[1] Univ Melbourne, Dept Chem & Biomol Engn, Melbourne, Vic 3010, Australia

[2] Univ Melbourne, Dept Biochem & Mol Biol, Melbourne, Vic 3010, Australia

[3] Univ Melbourne, Mol Sci & Biotechnol Inst Bio21, Melbourne, Vic 3010, Australia

[4] CSL Bioplasma, Dept Res & Dev, Broadmeadows, Vic 3047, Australia

来源：

SOFT MATTER | 2012年 / 8卷 / 02期

基金：

澳大利亚研究理事会;

关键词：

VON-WILLEBRAND-FACTOR; VONWILLEBRAND-FACTOR BINDING; AMYLOID FIBRIL FORMATION; SINGLE-POLYMER DYNAMICS; SIMPLE SHEAR-FLOW; FLEXIBLE POLYMERS; CONFORMATIONAL-CHANGES; PLATELET-AGGREGATION; MECHANICAL STABILITY; MOLECULAR-STRUCTURE;

D O I：

10.1039/c1sm06704d

中图分类号：

O64 [物理化学（理论化学）、化学物理学];

学科分类号：

070304 ; 081704 ;

摘要：

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 a-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.

引用

页码：385 / 389

页数：5

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