Wheat glutenin proteins assemble into a nanostructure with unusual structural features

Sarah H. Mackintosh, Susie J. Meade, Jackie P. Healy, Kevin H. Sutton, Nigel G. Larsen, Adam M. Squires, Juliet A. Gerrard

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25 Citations (SciVal)


The proteins of wheat have a known propensity to aggregate into a variety of forms. We report here a novel nanostructure from wheat proteins, derived from a crude extract of high molecular weight glutenins. The structure was characterised by a significant thioflavin T (ThT) fluorescence and a fibrillar morphology by transmission electron microscopy (TEM). The ThT fluorescence and TEM data are suggestive of an amyloid structure, but the X-ray fibre diffraction data show a reflection pattern (4.02, 4.2–4.3, 4.6, 12.9, 19.3 and 38.7 Å) inconsistent with both the classic amyloid form and the previously described β-helix structure. The 4.6 Å reflection is consistent with that predicted for the amyloid inter-β-strand, and the absence of the inter-β-sheet distance at ≈10–11 Å is not unprecedented in amyloid-like structures. However, our observed X-ray reflection pattern has not been previously reported and suggests a novel wheat glutenin nanostructure.
Original languageEnglish
Pages (from-to)157-162
JournalJournal of Cereal Science
Issue number1
Publication statusPublished - 1 Jan 2009


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