Atomic force microscopy was adopted to study the nanoscopic structure formation of natural fibrous protein, fibroin from the Samia cynthia ricini wild silkworm. We have observed highly ordered nanoscale textile-fabric-like structures of fibroin molecules. From AFM and SDS-PAGE experiments, it was revealed that fibroin molecules have a rigid rodlike structure and form aggregates by end-to-end interactions of molecules. By analogy with Bombyx mori fibroin, S. c. ricini fibroin is supposed to assemble by electrostatic interactions of molecules.
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