Nanomechanical force measurements of gliadin protein interactions

• Published in: Biopolymers 2006-12, Vol.83 (6), p.658-667
• Main Authors: Paananen, A., Tappura, K., Tatham, A. S., Fido, R., Shewry, P. R., Miles, M., McMaster, T. J.
• Format: Article
• Language: English
• Subjects: Acetic Acid; atomic force microscopy; force measurement; Gliadin - metabolism; gliadin interaction; gluten proteins; Microscopy, Atomic Force; Urea - metabolism
• ISSN: 0006-3525; 1097-0282
• DOI: 10.1002/bip.20603

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.© 2006 Wiley Periodicals, Inc. Biopolymers 83: 658–667, 2006 This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at [e-mail]