Puroindoline-a, a lipid binding protein from common wheat, spontaneously forms prolate protein micelles in solution

Clifton, L. A., Sanders, M. R., Castelletto, V., Rogers, S. E., Heenan, R. K., Neylon, C., Frazier, R. ORCID: https://orcid.org/0000-0003-4313-0019 and Green, R. J. (2011) Puroindoline-a, a lipid binding protein from common wheat, spontaneously forms prolate protein micelles in solution. Physical Chemistry Chemical Physics, 13 (19). pp. 8881-8888. ISSN 1463-9076 doi: 10.1039/c0cp02247k

Abstract/Summary

The self-assembly in solution of puroindoline-a (Pin-a), an amphiphilic lipid binding protein from common wheat, was investigated by small angle neutron scattering, dynamic light scattering and size exclusion chromatography. Pin-a was found to form monodisperse prolate ellipsoidal micelles with a major axial radius of 112 +/- 4.5 A ˚ and minor axial radius of 40.4 +/- 0.18 A ˚ . These protein micelles were formed by the spontaneous self-assembly of 38 Pin-a molecules in solution and were stable over a wide pH range (3.5–11) and at elevated temperatures (20–65 degC). Pin-a micelles could be disrupted upon addition of the non-ionic surfactant dodecyl-b-maltoside, suggesting that the protein self-assembly is driven by hydrophobic forces, consisting of intermolecular interactions between Trp residues located within a well-defined Trp-rich domain of Pin-a.

Item Type	Article
URI	https://reading-clone.eprints-hosting.org/id/eprint/19949
Item Type	Article
Refereed	Yes
Divisions	Life Sciences > School of Chemistry, Food and Pharmacy > School of Pharmacy > Pharmaceutics Research Group Life Sciences > School of Chemistry, Food and Pharmacy > Department of Chemistry Life Sciences > School of Chemistry, Food and Pharmacy > Department of Food and Nutritional Sciences > Food Research Group
Publisher	Royal Society of Chemistry
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