Multiplex Binding of Amyloid-like Protein Nanofilm to Different Material Surfaces

The development of a reliable universal way to form strongly bonded coating with underlying substrate independent on material chemistry is ideal surface modification strategy and remains great challenge. Recently developed polydopamine and amyloid-based adhesion systems are two representative examples reported so far to fulfill this aim, and nonetheless the universal surface adhesion mechanism in these two cases is still unclear up to now. Herein the systematical studies on the adhesive strength of the amyloid-like coating on metal, organic and inorganic material surfaces reveal a novel multiplex bonding model on polar and non-polar abiotic surfaces, and different binding mode for respective material chemical structure including metal-sulfur coordination bonding, hydrogen bonding, electrostatic and hydrophobic interaction is elucidated with affirmative bonding strength. Our findings lend insight into amyloid adhesion mechanisms and reveal strategies for theory-driven design of engineered adhesives that harness great promise for advanced materials and devices.