Trypsin hydrolysis of wheat gluten produced glutamine-rich short peptides with a tendency to self-assemble into supermolecular structures extrinsic to native wheat gluten. Fourier transform infrared and X-ray diffraction data suggested that the new structures formed resembled that of cross-β amyloid fibrils found in some insect silk and implicated in prion diseases. The superstructures were about 10 μm in diameter with clear right-handed helical configuration and appeared to be bundles of smaller fibrils of about 63 nm in diameter. Results demonstrate the potential for utilizing cheap protein sources and natural mechanisms of protein self-assembly to design advanced nanomaterials that can provide a wide range of structural and chemical functionality.
- Aerospace Division
Enzyme-Mediated Self-Assembly of Highly Ordered Structures From Disordered Proteins
- Views Icon Views
- Share Icon Share
- Search Site
Athamneh, A, & Barone, J. "Enzyme-Mediated Self-Assembly of Highly Ordered Structures From Disordered Proteins." Proceedings of the ASME 2008 Conference on Smart Materials, Adaptive Structures and Intelligent Systems. Smart Materials, Adaptive Structures and Intelligent Systems, Volume 2. Ellicott City, Maryland, USA. October 28–30, 2008. pp. 625-628. ASME. https://doi.org/10.1115/SMASIS2008-540
Download citation file: