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Nanoscale characterization of zein self-assembly.
- Source :
-
Langmuir : the ACS journal of surfaces and colloids [Langmuir] 2012 Feb 07; Vol. 28 (5), pp. 2429-35. Date of Electronic Publication: 2012 Jan 20. - Publication Year :
- 2012
-
Abstract
- Zein, a major protein of corn, is rich in α-helical structure. It has an amphiphilic character and is capable of self-assembly. Zein can self-assemble into various mesostructures that may find applications in food, agricultural, and biomedical engineering. Understanding the mechanism of zein self-assembly at the nanoscale is important for further development of zein structures. In this work, high-resolution transmission electron microscopy (TEM) images revealed nanosize zein stripes, rings, and discs containing a 0.35 nm periodicity, which is characteristic of β-sheet. TEM images were interpreted in terms of the transformation of original α-helices into β-sheet conformation after evaporation-induced self-assembly (EISA). The presence of β-sheet was also detected by circular dichroism (CD) spectroscopy. Zein β-sheets self-assembled into stripes, which curled into rings. Rings formed discs and eventually spheres. The formation of zein nanostructures was believed to be the result of β-sheet orientation, alignment, and packing.
Details
- Language :
- English
- ISSN :
- 1520-5827
- Volume :
- 28
- Issue :
- 5
- Database :
- MEDLINE
- Journal :
- Langmuir : the ACS journal of surfaces and colloids
- Publication Type :
- Academic Journal
- Accession number :
- 22224954
- Full Text :
- https://doi.org/10.1021/la204204j