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 pr otein molecules. The images showed fibrils with a diameter of between 15 an d 30 nm and lengths ranging from about 100 nm to 2 mu m. No branched fibril s were observed, and there was no indication of a strong lateral inter-fibr il interaction that would result in side-by-side association. Disassembly o f the fibrils occurred when the pH of the aqueous buffer was reduced. In co ntrast the reverse process of fibril assembly and adsorption to the mica su rface was less readily observed in situ. Some short fibrils were observed t o assemble, but the lengths and densities were considerably less than those obtained by external deposition and drying. (C) 2000 Academic Press.