title: Puroindoline-a, a lipid binding protein from common wheat, spontaneously forms prolate protein micelles in solution.
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.
authors: ISIS Spallation Neutron Source, Science and Technology Facilities Council, Rutherford Appleton Laboratory, Harwell Science and Innovation Campus, Didcot, OX11 0QX, UK. luke.clifton@stfc.ac.uk
authors: Luke A
authors: LA
authors: Clifton
authors: Michael R
authors: MR
authors: Sanders
authors: Valeria
authors: V
authors: Castelletto
authors: Sarah E
authors: SE
authors: Rogers
authors: Richard K
authors: RK
authors: Heenan
authors: Cameron
authors: C
authors: Neylon
authors: Richard A
authors: RA
authors: Frazier
authors: Rebecca J
authors: RJ
authors: Green
mesh_terms: D006863:Hydrogen-Ion Concentration; D008823:Micelles; D010940:Plant Proteins / Q000737:chemistry*; D012996:Solutions; D014908:Triticum / Q000737:chemistry*
chemical_list: D008823:Micelles; D010940:Plant Proteins; D012996:Solutions; C082942:puroindoline protein, Triticum aestivum