Atomic Force Microscopy of A-Gliadin Fibrils and in situ Degradation

Atomic force microscopy (AFM) has been used in air and in aqueous buffer to study the structure of fibrils formed by the self-assembly of A-gliadin protein molecules. The images showed fibrils with a diameter of between 15 and 30 nm and lengths ranging from about 100 nm to 2 μm. No branched fibrils...

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Veröffentlicht in:Journal of cereal science 2000-05, Vol.31 (3), p.281-286
Hauptverfasser: McMaster, T.J., Miles, M.J., Kasarda, D.D., Shewry, P.R., Tatham, A.S.
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container_end_page 286
container_issue 3
container_start_page 281
container_title Journal of cereal science
container_volume 31
creator McMaster, T.J.
Miles, M.J.
Kasarda, D.D.
Shewry, P.R.
Tatham, A.S.
description Atomic force microscopy (AFM) has been used in air and in aqueous buffer to study the structure of fibrils formed by the self-assembly of A-gliadin protein molecules. The images showed fibrils with a diameter of between 15 and 30 nm and lengths ranging from about 100 nm to 2 μm. No branched fibrils were observed, and there was no indication of a strong lateral inter-fibril interaction that would result in side-by-side association. Disassembly of the fibrils occurred when the pH of the aqueous buffer was reduced. In contrast the reverse process of fibril assembly and adsorption to the mica surface was less readily observed in situ. Some short fibrils were observed to assemble, but the lengths and densities were considerably less than those obtained by external deposition and drying.
doi_str_mv 10.1006/jcrs.2000.0307
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source ScienceDirect Journals (5 years ago - present)
subjects Animal, plant, fungal and microbial proteins, edible seaweeds and food yeasts
Biological and medical sciences
Food industries
Fundamental and applied biological sciences. Psychology
General aspects
gliadins, atomic force microscopy, scanning probe microscopy, A-gliadin fibrils, self-assembly
Methods of analysis, processing and quality control, regulation, standards
title Atomic Force Microscopy of A-Gliadin Fibrils and in situ Degradation
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