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Updated: Jun 29, 2026

Screening for Amyloid Aggregation by Semi-Denaturing Detergent-Agarose Gel Electrophoresis
Published on: July 17, 2008
Crack Suppression in Conductive Film by Amyloid-Like Protein Aggregation toward Flexible Device
Mengmeng Chen1, Facui Yang2, Xi Chen3
1Key Laboratory of Applied Surface and Colloid Chemistry, Ministry of Education, School of Chemistry and Chemical Engineering, Shaanxi Normal University, Xi'an, 710119, China.
Abstract:
A fatal weakness in flexible electronics is the mechanical fracture that occurs during repetitive fatigue deformation; thus, controlling the crack development of the conductive layer is of prime importance and has remained a great challenge until now. Herein, this issue is tackled by utilizing an amyloid/polysaccharide molecular composite as an interfacial binder. Sodium alginate (SA) can take part in amyloid-like aggregation of the lysozyme, leading to the facile synthesis of a 2D protein/saccharide hybrid nanofilm over an ultralarge area (e.g., >400 cm2 ). The introduction of SA into amyloid-like aggregates significantly enhances the mechanical strength of the hybrid nanofilm, which, with the help of amyloid-mediated interfacial adhesion, effectively diminishes the microcracks in the hybrid nanofilm coating after repetitive bending or stretching. The microcrack-free hybrid nanofilm then shows high interfacial activity to induce electroless deposition of metal in a Kelvin model on a substrate, which noticeably suppresses the formation of microcracks and consequent conductivity loss during the bending and stretching of the metal-coated flexible substrates. This work underlines the significance of amyloid/polysaccharide nanocomposites in the design of interfacial binders for reliable flexible electronic devices and represents an important contribution to mimicking amyloid and polysaccharide-based adhesive cements created by organisms.

