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.
Mackintosh, S. H., Meade, S. J., Healy, J. P., Sutton, K. H., Larsen, N. G., Squires, A. M., & Gerrard, J. A. (2009). Wheat glutenin proteins assemble into a nanostructure with unusual structural features. Journal of Cereal Science, 49(1), 157-162. https://doi.org/10.1016/j.jcs.2008.08.003