Identification of microphases in mixed alpha- and omega-gliadin protein films investigated by atomic force microscopy.
Pure and mixed films of alpha- and omega-gliadins were studied by tapping mode atomic force microscopy (AFM). The technique was sensitive to the chemistry of the surface properties of the films, allowing imaging of the mixed gliadin phases at different ratios. In addition to the study of the phases at the micrometer level, higher resolution images allowed visualization of the protein films at the molecular level. These studies may have relevance to the formation of phases in developing protein bodies in grain, where gliadins and glutenins are deposited together. It has been assumed that the protein bodies consist of a random network of proteins; these studies indicate that microphases could be present in protein bodies. The technique provides novel methods for studying mixed biopolymer systems.
McMaster
T J
TJ
H. H. Wills Physics Laboratory, University of Bristol, Tyndall Avenue, Bristol BS8 1TL, United Kingdom. t.mcmaster@bristol.ac.uk
Miles
M J
MJ
Wannerberger
L
L
Eliasson
A C
AC
Shewry
P R
PR
Tatham
A S
AS
D005903:Gliadin / Q000737:chemistry*; D018625:Microscopy, Atomic Force
D005903:Gliadin