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Issue 19, 2011
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Puroindoline-a, a lipid binding protein from common wheat, spontaneously forms prolate protein micelles in solution

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Abstract

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 Å and minor axial radius of 40.4 ± 0.18 Å. 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 °C). Pin-a micelles could be disrupted upon addition of the non-ionic surfactant dodecyl-β-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.

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

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Publication details

The article was received on 22 Oct 2010, accepted on 01 Mar 2011 and first published on 30 Mar 2011


Article type: Paper
DOI: 10.1039/C0CP02247K
Citation: Phys. Chem. Chem. Phys., 2011,13, 8881-8888
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    Puroindoline-a, a lipid binding protein from common wheat, spontaneously forms prolate protein micelles in solution

    L. A. Clifton, M. R. Sanders, V. Castelletto, S. E. Rogers, R. K. Heenan, C. Neylon, R. A. Frazier and R. J. Green, Phys. Chem. Chem. Phys., 2011, 13, 8881
    DOI: 10.1039/C0CP02247K

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