Nanomechanical force measurements of gliadin protein interactions

Arja Paananen, Kirsi Tappura, A. S. Tatham, R. Fido, P. R. Shewry, M. Miles, T. J. McMaster (Corresponding Author)

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Abstract

The strength and nature of interactions between monomeric gliadin proteins involving α–α, ω–ω, and α–ω interactions in 0.01M acetic acid, and the effect of urea has been investigated. It was shown by means of nanomechanical force measurements that the stretching events in the separation curve after adhesive phenomena originated from proteins. These stretching events displayed different responses of the α‐ and ω‐gliadins to urea. While 2M urea caused the more globular α‐gliadins to unfold, the β‐turn‐rich ω‐gliadins remained fairly stable even in 8M urea. This suggests different roles for gliadins in the formation of dough; while the ω‐gliadins are still in a compact structure being responsible for the viscous flow, the α‐gliadins have already started to participate in forming the network in dough.
Original languageEnglish
Pages (from-to)658-667
Number of pages10
JournalBiopolymers
Volume83
Issue number6
DOIs
Publication statusPublished - 2006
MoE publication typeA1 Journal article-refereed

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Keywords

  • atomic force microscopy
  • force measurement
  • gliadin interaction
  • gluten proteins

Cite this

Paananen, A., Tappura, K., Tatham, A. S., Fido, R., Shewry, P. R., Miles, M., & McMaster, T. J. (2006). Nanomechanical force measurements of gliadin protein interactions. Biopolymers, 83(6), 658-667. https://doi.org/10.1002/bip.20603