Unfolding and refolding of bovine serum albumin at acid pH: Ultrasound and structural studies

N. El Kadi, N. Taulier, J. Y. Le Huérou, M. Gindre, W. Urbach, I. Nwigwe, P. C. Kahn, M. Waks

Research output: Contribution to journalArticle

130 Citations (Scopus)

Abstract

Serum albumin is the most abundant protein in the circulatory system. The ability of albumins to undergo a reversible conformational transition, observed with changes in pH, is conserved in distantly related species, suggesting for it a major physiological role possibly related to the transport of small molecules including drugs. We have followed changes of bovine serum albumin (BSA) in volume by densimetry and in adiabatic compressibility during its conformational transition from pH 7-2, using ultrasound measurements. In parallel, circular dichroism was measured. The volume and adiabatic compressibility decrease from pH 4 to 2. The change in ellipticity shows a decrease over the same pH range from 70% to 40% of its α-helix content. Sorbitol, at concentrations from 0 to 2 M, led to the progressive restoration of BSA volume and compressibility values, as well as a substantial recovery of its original α-helix content. This finding implies that the compressibility variation observed reflects the conformational changes during the transition. The mutual interactions of the mechanical properties and structural features of BSA reported here are important in biotechnology for research in material sciences and for the design and the development of new, tailor-made drug carriers.

Original languageEnglish (US)
Pages (from-to)3397-3404
Number of pages8
JournalBiophysical Journal
Volume91
Issue number9
DOIs
StatePublished - Nov 2006

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Bovine Serum Albumin
Acids
Drug Carriers
Sorbitol
Biotechnology
Circular Dichroism
Cardiovascular System
Serum Albumin
Albumins
Research
Pharmaceutical Preparations
Proteins

All Science Journal Classification (ASJC) codes

  • Biophysics

Cite this

El Kadi, N., Taulier, N., Le Huérou, J. Y., Gindre, M., Urbach, W., Nwigwe, I., ... Waks, M. (2006). Unfolding and refolding of bovine serum albumin at acid pH: Ultrasound and structural studies. Biophysical Journal, 91(9), 3397-3404. https://doi.org/10.1529/biophysj.106.088963
El Kadi, N. ; Taulier, N. ; Le Huérou, J. Y. ; Gindre, M. ; Urbach, W. ; Nwigwe, I. ; Kahn, P. C. ; Waks, M. / Unfolding and refolding of bovine serum albumin at acid pH : Ultrasound and structural studies. In: Biophysical Journal. 2006 ; Vol. 91, No. 9. pp. 3397-3404.
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El Kadi, N, Taulier, N, Le Huérou, JY, Gindre, M, Urbach, W, Nwigwe, I, Kahn, PC & Waks, M 2006, 'Unfolding and refolding of bovine serum albumin at acid pH: Ultrasound and structural studies', Biophysical Journal, vol. 91, no. 9, pp. 3397-3404. https://doi.org/10.1529/biophysj.106.088963

Unfolding and refolding of bovine serum albumin at acid pH : Ultrasound and structural studies. / El Kadi, N.; Taulier, N.; Le Huérou, J. Y.; Gindre, M.; Urbach, W.; Nwigwe, I.; Kahn, P. C.; Waks, M.

In: Biophysical Journal, Vol. 91, No. 9, 11.2006, p. 3397-3404.

Research output: Contribution to journalArticle

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AU - El Kadi, N.

AU - Taulier, N.

AU - Le Huérou, J. Y.

AU - Gindre, M.

AU - Urbach, W.

AU - Nwigwe, I.

AU - Kahn, P. C.

AU - Waks, M.

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